Leucine Rich Repeat
Leucine Rich Repeat - Related Videos
11:31
Metabolic Labeling of Leucine Rich Repeat Kinases 1 and 2 with Radioactive Phosphate
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Cited by 5 •
2013
Leucine rich repeat kinases 1 and 2 (LRRK1 and LRRK2) are multidomain proteins which encode both GTPase and kinase domains and which are phosphorylated in cells. Here, we present a protocol to label LRRK1 and LRRK2 in cells with 32P orthophosphate, thereby providing a means to measure their overall cellular phophorylation levels.
08:54
Monitoring Leucine-Rich Repeat Containing 8 Channel (LRRC8/VRAC) Activity Using Sensitized-Emission Förster Resonance Energy Transfer (SE-FRET)
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2024
Electrophysiology is the gold standard for investigating ion channel activity. However, there are plenty of alternative approaches, including optical methods. Here, we describe a method to monitor the activity of the leucine-rich repeat containing 8 channel (LRRC8)-formed anion channels using an inter-subunit Förster resonance energy transfer (FRET)-based method.
01:28
Infinitely Repeated Games
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2025
An infinitely repeated game is a scenario where players repeatedly engage in the same game without a predetermined end. This concept is crucial in understanding long-term interactions in various fields of the social sciences, including economics and international relations. Examples: Firms Setting Prices: Companies continuously adjust prices. Trade Negotiations: Countries consistently negotiate trade terms. Tit-for-Tat Strategy Cooperative Start: Players begin with a cooperative action,...
01:20
Finitely Repeated Games
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2025
Repeated games are scenarios where the same game is played multiple times by the same participants. These games are fundamental in understanding how decision-making processes evolve over time. Finitely Repeated Games: These games occur a specific number of times. Consider two software firms that are in competition, releasing updates to their software every quarter. Each quarter, these firms must decide on their strategic approach: they can either invest heavily in developing innovative new...
07:48
Within-subjects Repeated-measures Design
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2023
Source: Laboratories of Gary Lewandowski, Dave Strohmetz, and Natalie Ciarocco—Monmouth University A within-subjects, or repeated-measures, design is an experimental design where all the participants receive every level of the treatment, i.e., every independent variable. For example, in a candy taste test, the researcher would want every participant to taste and rate each type of candy. This video demonstrates a within-subjects experiment (i.e., one where there is an independent variable with...
FAQs
The repeats assemble into a curved, horseshoe-shaped domain rather than acting as isolated sequence elements. This arrangement places a parallel beta-sheet along the inner surface and alpha-helices on the outer surface, creating an organized interaction framework. The resulting geometry helps present exposed residues in a position suitable for recognizing proteins, peptides, or other ligands.
Although the repeats share a leucine-rich pattern, residues exposed on the interaction surface can vary. Those differences help determine which molecular partners fit the domain and support selective recognition. In signaling and immune-related proteins, this surface variability allows related domains to participate in distinct protein, peptide, or ligand interactions without changing the overall curved architecture.
The curved fold provides an extended surface for molecular contacts, while its organized beta-sheet and alpha-helical regions help maintain domain stability. When exposed residues engage a binding partner, the domain can contribute to recognition events that connect extracellular or intracellular signals to cellular responses. This structural organization is therefore relevant to protein-protein interactions and signaling pathways.
Structural stability is associated with the conserved repeat framework and the arrangement of the beta-sheet and alpha-helices. Recognition specificity depends more strongly on variable residues exposed to the surrounding molecular environment. Examining both features helps researchers determine whether a domain primarily preserves its fold, selects a particular ligand, or performs both functions during molecular recognition.
These domains occur in immune receptors, intracellular signaling proteins, and plant disease-resistance proteins. Their presence across these systems links a shared structural strategy to different biological contexts: detecting molecular signals, transmitting information inside cells, and contributing to plant responses associated with disease resistance. Studying the domain in each setting reveals how recognition supports distinct cellular outcomes.
In immune receptors and plant disease-resistance proteins, exposed residues provide interaction surfaces that can recognize relevant proteins, peptides, or other ligands. Such binding contributes to pathogen detection and the initiation of molecular responses. Comparing these domains across immune and plant systems helps connect protein structure with recognition, cellular communication, and the molecular basis of immune responses.