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Related Concept Videos

Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

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Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to...
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Conserved Binding Sites01:49

Conserved Binding Sites

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Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
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Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

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Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
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The membrane domains concentrate specific lipids and proteins at one place within the membrane, which helps in cell signaling, adhesion, and other critical cellular processes. These domains can differ in size, composition, function, and lifespan.
Protein Domains
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Ligand Binding and Linkage00:49

Ligand Binding and Linkage

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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 sites. When a protein is allosteric, its binding sites are called coupled or linked.  In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence...
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Updated: Sep 23, 2025

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues
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SRC homology 3 domains: multifaceted binding modules.

Ugo Dionne1, Lily J Percival2, François J M Chartier1

  • 1Centre de recherche sur le cancer et Centre de recherche du CHU de Québec - Université Laval, QC, Canada; Quebec Network for Research on Protein Function, Engineering, and Applications (PROTEO), QC, Canada.

Trends in Biochemical Sciences
|May 13, 2022
PubMed
Summary
This summary is machine-generated.

SRC homology (SH)3 domains are key signaling proteins. Recent findings reveal their complex roles in protein interactions, challenging the simple portable domain model.

Keywords:
SH3 domainsliquid–liquid phase separationphosphorylationprotein contextprotein–protein interactionssignaling

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Area of Science:

  • Molecular Biology
  • Cell Signaling
  • Protein Interactions

Background:

  • Signaling proteins with multiple peptide binding modules control complex assembly after extracellular signal detection.
  • SRC homology (SH)3 domains are archetypal modular protein interaction modules, with ~300 annotated human SH3 domains regulating diverse signaling processes.

Purpose of the Study:

  • To review recent findings on SRC homology (SH)3 domains.
  • To challenge the traditional view of SH3 domains as simple portable binding modules.

Main Methods:

  • Literature review of recent research on SH3 domains.

Main Results:

  • SH3 domains exhibit allosteric contributions influenced by host protein context.
  • Phosphorylation significantly impacts SH3 domain function.
  • SH3 domains play roles in phase separation, indicating complex regulatory mechanisms.

Conclusions:

  • The function of SH3 domains is more intricate than previously thought, involving context-dependent allostery, phosphoregulation, and phase separation.
  • A revised model is needed to fully understand the regulatory roles of SH3 domains in cellular signaling.