Name: antibody heavy and light chains
Uploaded: 2020-11-23T11:47:34.000Z
Duration: 1 min 10 s
Channel: JoVE

K12 Standards

Tennessee Academic Standards

High School

Biology

from-molecules-to-organisms-structures-and-processes

From Molecules to Organisms: Structures and Processes

BIO1.LS1.3

Antibody Structure

Przeciwciała, znane również jako immunoglobuliny, odgrywają kluczową rolę w humoralnej odpowiedzi immunologicznej przeciwko obcym antygenom.
Są to białka, które składają się z czterech polipeptydów w strukturze w kształcie litery Y. Z dwoma identycznymi ciężkimi i dwoma identycznymi lekkimi łańcuchami. Połączone ze sobą poprzez połączenie wiązań niekowalencyjnych i kowalencyjnych wiązań dwusiarczkowych.
Na samych końcach każdego łańcucha polipeptydowego znajdują się unikalne zmienne domeny, które selektywnie wiążą antygeny. Podczas gdy niektóre części tego regionu oddziałują bezpośrednio, inne części zapewniają strukturalne wsparcie dla tych miejsc wiązania.
Natomiast region macierzysty przeciwciała, znany jako region stały, określa specyficzny immunologiczny mechanizm działania w zależności od klasy.
Na przykład jeden rodzaj, immunoglobulina E, jest wydzielany w organizmie w odpowiedzi na alergen, taki jak sierść kota, i pośredniczy w reakcji alergicznej.

Silverton, E. W., M. A. Navia i D. R. Davies. "Trójwymiarowa struktura nienaruszonej ludzkiej immunoglobuliny". Proceedings of the National Academy of Sciences 74, nr 11 (1 listopada 1977): 5140–44. [<a href="https://doi.org/10.1073/pnas.74.11.5140" target="__blank">Źródło</a>]

struktura przeciwciał

<h4>Przegląd</h4>

Przeciwciała, znane również jako immunoglobuliny (Ig), odgrywają kluczową rolę w nabytym układzie odpornościowym. Te białka wiążące antygen są wytwarzane przez limfocyty B i stanowią 20 procent masy całkowitego osocza krwi. U ssaków przeciwciała dzielą się na pięć różnych klas, z których każda wywołuje inną odpowiedź biologiczną po związaniu antygenu.

<h4>Struktura przeciwciał w kształcie litery Y składa się z czterech łańcuchów polipeptydowych</h4>

Przeciwciała składają się z czterech łańcuchów polipeptydowych: dwóch identycznych łańcuchów ciężkich, każdy o długości około 440 aminokwasów, i dwóch identycznych łańcuchów lekkich, o długości około 220 aminokwasów każdy. Łańcuchy te są ułożone w strukturę w kształcie litery Y, która jest utrzymywana razem przez kombinację kowalencyjnych wiązań dwusiarczkowych i wiązań niekowalencyjnych. Ponadto większość przeciwciał zawiera reszty cukrowe. Proces dodawania cukrowych łańcuchów bocznych do białka nazywa się glikozylacją.

<h4>Podjednostki przeciwciała mają różne funkcje</h4>

Zarówno łańcuch lekki, jak i łańcuch ciężki biorą udział w miejscu wiązania antygenu na każdym z końców struktury Y. Te 110–130 aminokwasów charakteryzują się dużą zmiennością, co pozwala na rozpoznanie niemal nieograniczonej liczby antygenów. Region ten nazywany jest także regionem zmiennym i stanowi część fragmentu wiążącego antygen.

Każde ramię jednostki w kształcie litery Y zawiera identyczne miejsce wiązania antygenu. Przeciwciała mogą sieciować antygeny: gdy jedno ramię wiąże się z jednym antygenem, a drugie ramię wiąże się z drugim, strukturalnie identycznym antygenem. Sieciowanie jest ułatwione dzięki elastycznemu regionowi zawiasowemu, który łączy ramiona przeciwciała z łodygą i umożliwia zmienne odległości pomiędzy miejscami wiązania antygenu. Duże sieci usieciowanych antygenów są następnie szybciej i łatwiej wchłaniane przez makrofagi, usuwając jednocześnie większe ilości antygenu.

Region łodygi przeciwciała nazywany jest także regionem ulegającym krystalizacji fragmentu (Fc) i określa funkcję efektorową przeciwciała. Za pośrednictwem domeny Fc przeciwciało może oddziaływać z receptorami Fc na innych komórkach układu odpornościowego, takich jak komórki B, makrofagi i komórki tuczne. Region Fc jest często glikozylowany, co utrudnia lub umożliwia dostęp do receptora Fc. Zmiana stanu glikozylacji przeciwciała umożliwia zatem szybką modulację funkcji przeciwciała.

<h4>Ssaki mają pięć klas przeciwciał</h4>

Przeciwciała są klasyfikowane według liczby struktur w kształcie litery Y i rodzaju łańcuchów ciężkich. Przeciwciała klasy IgD, IgE i IgG mają pojedynczą strukturę w kształcie litery Y, zapewniającą dwa identyczne miejsca wiązania antygenu na końcach ramion. Mówiąc bardziej naukowo: mają wartościowość równą dwa. IgD, IgE i IgG różnią się jednak składem wiązań dwusiarczkowych i niekowalencyjnych pomiędzy ich dwoma łańcuchami ciężkimi. IgA może występować jako monomer lub dimer, przypominając dwa Y połączone zasadą. Jako dimer, IgA ma cztery identyczne miejsca wiązania antygenu — wartościowość wynosi cztery. IgM może występować jako monomer, ale częściej występuje w postaci pentameru, co nadaje jej wartościowość 10.

<h4>Pięć klas przeciwciał wyzwala różne funkcje odpornościowe</h4>

Przeciwciała IgG są najliczniejszymi cząsteczkami przeciwciał we krwi i są wydzielane w dużych ilościach, gdy po raz drugi spotyka się określony patogen. IgG przyczyniają się do eliminacji patogenów na kilka sposobów. Opsonizują patogeny, wywołując fagocytozę przez makrofagi lub neutrofile. Aktywność tych komórek fagocytarnych jest wzmacniana przez układ dopełniacza, kaskadę białek enzymatycznych. Układ dopełniacza sam jest wyzwalany przez IgG. Co więcej, IgG są jedynymi przeciwciałami, które mogą przenikać przez łożysko od matki do płodu. Są one również wydzielane do mleka matki, zapewniając w ten sposób odporność bierną, która chroni niemowlę przed infekcjami.

Monomery klasy IgM jako pierwsze pojawiają się na naiwnych komórkach B. IgM to główna klasa przeciwciał wydzielanych przez limfocyty B w odpowiedzi na pierwszą ekspozycję na antygen — pierwotna odpowiedź przeciwciał. Kiedy antygen wiąże się z cząsteczką IgM, aktywuje układ dopełniacza i neutralizuje patogeny.

Funkcje przeciwciał IgD nie są dobrze poznane, ale wydają się przypominać funkcje przeciwciał IgM.

IgE są trudne do zbadania ze względu na ich niski poziom w płynach ustrojowych i są znane głównie z ich negatywnego wpływu na dobrostan człowieka: alergii. Podczas reakcji alergicznej IgE wiąże się ze swoim pokrewnym antygenem. Następnie region Fc IgE wiąże się z komórkami tucznymi i bazofilami, rodzajem białych krwinek. Interakcja IgE i receptora Fc na powierzchni komórki powoduje uwalnianie histamin i interleukin, co z kolei powoduje objawy alergiczne, takie jak kichanie i swędzenie.

<h4>Przeciwciała do celów badawczych, diagnostycznych i terapeutycznych są produkowane u zwierząt</h4>

Przeciwciała są ważnym narzędziem w wielu dyscyplinach naukowych, a także w diagnostyce, a czasami w leczeniu chorób. Aby wytworzyć przeciwciała, antygen wstrzykuje się zwierzęciu hodowlanemu lub laboratoryjnemu, często królikom, kurczakom, chomikom lub kozom, a następnie izoluje się z krwi zwierzęcia.

Struktura przeciwciał

Przegląd
Przeciwciała, znane również jako immunoglobuliny (Ig), są niezbędnymi uczestnikami adaptacyjnego układu odpornościowego. Te białka wiążące antygen są wytwarzane ...

Education

JoVE Core

Molecular Biology

Biologia molekularna

Unit 1

Jednostka 1

Protein Structure

Struktura białek

KEY TERMS AND CONCEPTS

Kluczowe terminy i pojęcia

antibody heavy and light chains

Antibodies are built from heavy and light chains that work together to form a Y-shaped molecule. These chains give the antibody its basic structure and help it bind to specific targets.

The two upper arms of the Y contain the variable regions, which differ from one antibody to another. These variable regions help determine which antigen, or foreign molecule, the antibody can recognize.

The lower part of the antibody is the constant region. This region is more similar across antibodies and helps define the antibody class. The structure of the chains also supports the antibody’s overall shape and function.

Antibody Heavy and Light Chains

what are proteins?

Proteins, Amino Acids, and Polypeptides

Proteins are built from amino acids and form polypeptides. Amino acids are the small building blocks, and a polypeptide is a chain of amino acids joined together. This basic relationship explains how proteins are made and why their structure matters. Proteins have several important roles in living things. Some proteins help build body structures, while others carry out work inside cells. The transcript also connects proteins to enzymes, which are proteins that speed up chemical reactions.

protein organization

Protein Organization and Folding Levels

Protein organization describes how a protein is arranged at several levels. These levels help explain how a chain of amino acids becomes a working molecule. The main stages are primary, secondary, tertiary, and quaternary structure. Primary structure is the linear order of amino acids in the protein chain. Secondary structure is the first step of folding. In this stage, the chain can form patterns such as helices and sheets. Tertiary structure is the overall three-dimensional shape of one...

protein folding

Protein Folding and Structure

Protein folding is the process that gives a protein its final three-dimensional shape. That shape is essential because a protein’s structure helps determine how it works in the cell. A folded protein is stabilized by several interactions. These include hydrogen bonds, van der Waals interactions, and disulfide bridges. Each one helps hold the protein in the correct form. When a protein does not fold properly, its structure can change. That can affect its function and can interfere with normal...

conservation of protein domains over different proteins

conservation-of-protein-domains-over-different-proteins

Argonaute Protein Domains Across Species

Argonaute proteins have conserved domains that help small RNAs guide gene silencing. These proteins are found across organisms, but the number of Argonaute family members can differ from one species to another. Protein domains are small, structurally independent parts of a single amino acid chain. They can keep their shape on their own, but they may still work together with other parts of the protein. During evolution, domains can duplicate, recombine, and form new combinations. This process,...

globular and fibrous proteins

Protein Shapes: Globular vs Fibrous

Proteins can be grouped by shape into globular proteins and fibrous proteins. These two subtypes also differ in how they dissolve in water and in the jobs they do in cells and tissues. Globular proteins, also called spheroproteins, are usually round in shape. They contain a mix of amino acid types and varied primary sequences. Their shapes support many functions, including enzymes, cellular messengers, and molecular transporters. These roles often need the proteins to stay soluble in the...

intrinsically disordered proteins

Flexible Protein Regions and Binding

Intrinsically disordered proteins are proteins that do not fold into one fixed three-dimensional shape. Their flexible structure helps them work with ordered proteins to do jobs that rigid proteins cannot easily do. They are found more often in eukaryotes than in prokaryotes, and they can be fully disordered or made of both ordered and disordered regions. This lack of a rigid shape is linked to amino acid makeup. These proteins usually have many polar and charged amino acids and fewer...

protein complex assembly

How Proteins Self-Assemble in Cells

Proteins can self-assemble into working complexes inside cells. Some complexes are homomeric, which means they contain more than one copy of the same protein. Others are heteromeric, which means they are built from different protein types. Most protein complexes form through ordered self-assembly. In some cases, assembly factors help guide the proteins into the correct structure. Even in the crowded space inside a cell, proteins usually find the right partners and form functional complexes. <br...

conjugated proteins

Conjugated Proteins and Their Roles

Conjugated proteins are proteins that bond with a non-protein part. Unlike simple proteins, which contain only amino acids, these protein complexes include another chemical moiety attached covalently. That extra part can change how the protein works in the body. Nucleoproteins are conjugated proteins that contain nucleic acids. They are grouped as deoxyribonucleoproteins (DNPs) or ribonucleoproteins (RNPs). A nucleosome is a common DNP example, where nuclear DNA is associated with histone...

amyloid fibrils

Amyloid Fibrils in Brain Disease

Amyloid fibrils are clumps of misfolded proteins linked to brain disease and other disorders. In normal cells, misfolded proteins are usually refolded by chaperone proteins or broken down by the proteasome. But in some mutations or diseases, these proteins can build up into large clusters and then assemble into long fibers called fibrils. Amyloid deposits were seen as early as 1639 in the liver and spleen. In 1854, Rudolph Virchow used iodine staining, a method normally used to identify...

antibody structure

Antibodies are built from heavy and light chains that work together to form a Y-shaped molecule. These chains give the antibody its basic structure and help it bind to specific targets. The two upper arms of the Y contain the variable regions, which differ from one antibody to another. These variable regions help determine which antigen, or foreign molecule, the antibody can recognize. The lower part of the antibody is the constant region. This region is more similar across antibodies and...

protein families

Protein Families and Superfamilies

Protein families are groups of homologous proteins with similar amino acid sequences and three-dimensional shapes. They often appear after gene duplication, when an extra copy of a gene is added to an organism’s genome. Mutations can then change the amino acids, as long as the protein can still be made correctly. If the new proteins keep similar amino acids in key places, their domains and overall three-dimensional structure can stay similar too. Members of the same family can share as little...

key terms and concepts

Explore how antibody heavy and light chains form a Y-shaped molecule, with variable regions for target binding and a constant region that helps define class.

Antibody Heavy and Light Chains | JoVE K12

molecular biology

JoVE Core Molecular Biology showcases the molecular processes of the cell through clear and concise animated video lessons. Additionally, in scientist-in-action videos, these concepts' application is demonstrated through real experiments in modern laboratories.

Arizona Science Standards

Life Science

HS+B.L1

HS+B.L1U1.5

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Characteristics of Life

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the-tree-of-life-bacteria-archaea-and-eukaryotes

The Tree of Life - Bacteria, Archaea, and Eukaryotes

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Compare and contrast existing models, identify patterns, and use structural and functional evidence to analyze the characteristics of life. Engage in argument about the designation of viruses as non-living based on these characteristics.
EXPLANATION: Students begin to develop patterns of living and non-living organisms in kindergarten and build on detailed characteristics of different classifications of living organisms throughout elementary and middle school. Biology 1 discussions introduce viral particles and viral cycles, building on student understanding of living organisms to engage in an argument regarding the classification of a viral particle as either living or non-living.

BIO1.LS1.1

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Eukaryotic Compartmentalization

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Evaluate comparative models of various cell types with a focus on organic molecules that make up cellular structures.
EXPLANATION: Students explicitly discuss the structure and function of major cellular organelles in seventh grade. Building on this understanding, Biology I students should shift their focus to the different types of cells found in organisms and how the role of each cell type relates to its composition and the prevalence of different organelles within that cell. An example might include the absence (or enucleation) of the nucleus in red blood cells in mammals providing for increased levels of oxygen transport in organisms or the lack of centrioles in most neurons. Varying cell types can include both prokaryotic and eukaryotic cell types.

BIO1.LS1.2

Nucleic Acids

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DNA Base Pairing

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The Central Dogma

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DNA Packaging

Overview

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Organization of Genes

Overview

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Karyotyping

Describing the number and physical features of chromosomes can reveal abnormalities that underlie genetic diseases. This description is facilitated by ...

Replication in Prokaryotes

Overview

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Replication in Eukaryotes

Overview

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Mutations

Overview

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Transcription

Overview
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Translation

Lesson: Translation
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RNA Structure

Overview
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RNA Stability

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pre-mRNA Processing

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Types of RNA

Overview
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MicroRNAs

siRNA - Small Interfering RNAs

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piRNA - Piwi-interacting RNAs

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CRISPR and crRNAs

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lncRNA - Long Non-coding RNAs

In humans, more than 80% of the genome gets transcribed. However, only around 2% of the genome codes for proteins. The remaining part produces non-coding ...

What are Proteins?

Protein Organization

Protein Folding

Protein Families

Protein families are groups of homologous proteins; that is, they have similarities in amino acid sequences and three-dimensional structures. Protein ...

Conservation of Protein Domains Over Different Proteins

Protein domains are small structurally independent units that are part of a single amino acid chain.&#160; Although these domains are often structurally ...

Globular and Fibrous Proteins

Many proteins can be classified into two distinct subtypes - globular or fibrous. These two types differ in their shapes and solubilities.
Globular ...

Intrinsically Disordered Proteins

Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows ...

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.&#160; Most protein complexes ...

Conjugated Proteins

Simple proteins and protein complexes contain only amino acids. In contrast, many other proteins, called conjugated proteins, covalently bond with ...

Allosteric Proteins-ATCase

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Amyloid Fibrils

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Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand ...

Phosphorylation

Ligand Binding Sites

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Protein Kinases and Phosphatases

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Protein-protein Interfaces

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GTPases and their Regulation

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Conserved Binding Sites

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Covalently Linked Protein Regulators

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The Equilibrium Binding Constant and Binding Strength

The equilibrium binding constant (Kb) quantifies the strength of a protein-ligand interaction. Kb can be calculated as follows when the reaction is at ...

protein-complexes-with-interchangeable-parts

Protein Complexes with Interchangeable Parts

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Cofactors and Coenzymes

Mechanical Protein Functions

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Allosteric Regulation

Structural Protein Function

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Ligand Binding and Linkage

Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other ...

Protein Networks

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Integrate evidence to develop a structural model of a DNA molecule. Using the model, develop and communicate an explanation for how DNA serves as a template for self-replication and encodes biological information.
EXPLANATION: Discussions of DNA in earlier grades have been limited to discussions of genes and the role of genes in the appearance and activities of an organism. Biology 1 represents a student's introduction to a molecular model of a DNA as well as the organization of DNA into genes and genes subsequently into chromosomes. Students should address interactions between genes in proteins which regulate both the shape and reproduction of DNA molecules. It is important to note that not all segments of DNA are transcribed for proteins. Portions of DNA are involved in regulating the expression of genes or affect the structure of the chromosomes (replication origin, centromeres, and telomeres).

What is the Cell Cycle?

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Interphase

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The Cell Cycle Control System

Positive Regulator Molecules

Inhibition of CDK Activity

S-Cdk Initiates DNA Replication

M-Cdk Drives Transition Into Mitosis

Mitogens and the Cell Cycle

Replicative Cell Senescence

Abnormal Proliferation

cells-coordinate-growth-and-proliferation

Cells Coordinate Growth and Proliferation

Create a model for the major events of the eukaryotic cell cycle, including mitosis. Compare and contrast the rates of cell division in various eukaryotic cell types in multicellular organisms.
EXPLANATION: Students first discuss mitosis in seventh grade, specifically focusing on the role of mitosis in creating genetically identical daughter cells. Biology 1 discussions should connect a student's understanding of gene expression and protein function with the process of mitosis to explore the differentiation of cell types from otherwise identical daughter cells. Discussions should also include varying rates of mitotic division and the relationship between these rates of division and the function of specific cell types within eukaryotic organisms. Examples may include the extremely limited use of mitosis by neurons due to their interconnectedness within neural networks or the rapid rates of mitosis with growing root tips.

BIO1.LS1.6

Antibody Heavy and Light Chains

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