Cell Surface Receptor Binding
Cell Surface Receptor Binding - Related Videos
01:28
Types of Receptors: Cell Surface Receptors
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2023
Cell-surface receptors, also known as transmembrane receptors, are cell surface, membrane-anchored (integral) proteins that bind to external ligand molecules. This type of receptor spans the plasma membrane and performs signal transduction, converting an extracellular signal into an intracellular signal. Ligands that interact with cell-surface receptors do not have to enter the cell that they affect. Cell-surface receptors are also called cell-specific proteins or markers because they are...
04:55
Assaying Surface Expression of Chemosensory Receptors in Heterologous Cells
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Cited by 6 •
2011
Here we demonstrate a protocol to carry out live cell staining that can be used to detect odorant receptors on the surface of HEK293T cells conveniently. In addition, it may also be used to assay for surface expression of other chemosensory receptors or GPCRs.
08:49
Cell Surface Receptor Identification Using Genome-Scale CRISPR/Cas9 Genetic Screens
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Cited by 8 •
2020
This manuscript describes a genome-scale cell-based screening approach to identify extracellular receptor-ligand interactions.
06:27
Competitive Binding Assay to Identify Compounds Disrupting Receptor-Ligand Interactions
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2025
In this video, we describe a flow cytometry-based competitive binding assay to detect the interactions between the CXC Chemokine Receptor 4 (CXCR4) and its fluorescently-labeled natural ligand CXC Chemokine Ligand 12 (CXCL12), in the presence of a CXCR4-targeting small molecule. Incubating CXCR4-expressing cells with lower small molecule concentrations allows CXCR4-CXCL12 binding to some extent, which progressively declines upon a gradual increase in small molecule concentrations.
10:13
Measuring G-protein-coupled Receptor Signaling via Radio-labeled GTP Binding
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Cited by 11 •
2017
Guanosine triphosphate (GTP) binding is one of the earliest events in G-Protein-Coupled Receptor (GPCR) activation. This protocol describes how to pharmacologically characterize specific GPCR-ligand interactions by monitoring the binding of the radio-labeled GTP analog, [35S]guanosine-5'-O-(3-thio)triphosphate ([35S]GTPγS), in response to a ligand of interest.
FAQs
Binding can alter the receptor’s conformation, meaning its three-dimensional arrangement changes after ligand engagement. That structural shift can initiate signaling inside the cell, linking recognition at the membrane to a cellular response. In immunology, this mechanism helps explain how contact with an antigen or signaling molecule can regulate immune activation rather than serving only as a physical attachment event.
Molecular complementarity allows a ligand and receptor to fit selectively through matching structural features. Noncovalent forces help stabilize that interaction without forming a permanent chemical bond. Together, these properties help determine which molecules can engage a receptor and support selective communication between immune cells, host tissues, and infectious agents.
Both interactions depend on selective molecular recognition, but their consequences can differ. Immune receptors may bind antigens or signaling molecules to promote communication and immune activation. Pathogens can instead exploit host receptors for attachment and entry into cells. Comparing these outcomes helps distinguish protective recognition from receptor engagement that may contribute to infection and disease progression.
Analyzing these interactions can clarify how immune receptors recognize antigens, how signaling molecules regulate immune responses, and how pathogens identify suitable host cells. The resulting information connects molecular recognition with host-pathogen recognition and disease progression. It can therefore help researchers explain why receptor engagement produces particular immune or infectious outcomes.
Assays provide a way to study whether a ligand engages its cell surface receptor and to examine the selectivity of that interaction. In infection and immunology research, they can support analysis of immune recognition or pathogen attachment. Such studies also help evaluate strategies intended to block harmful receptor-ligand interactions that contribute to host-cell entry or disease.
Blocking can be useful when receptor engagement promotes an undesirable outcome, such as pathogen attachment or entry into host cells. Studying inhibition helps determine whether that interaction is necessary for the infectious process and supports development of interventions that interrupt it. The same experimental logic can also clarify which receptor-ligand contacts are most important in disease progression.