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Related Concept Videos

Protein-protein Interfaces02:04

Protein-protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...
Protein Networks02:26

Protein Networks

An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...

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Primer-Free Aptamer Selection Using A Random DNA Library
11:14

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Published on: July 26, 2010

Unique S100 target protein interactions.

Atoosa Rezvanpour1, Gary S Shaw

  • 1Department of Biochemistry, University of Western Ontario, London, Ontario, Canada N6A 5C1.

General Physiology and Biophysics
|January 23, 2010
PubMed
Summary
This summary is machine-generated.

Calcium binding induces conformational changes in S100 proteins, enabling interactions with biological targets. This review explores multiprotein complexes involving calcium-insensitive S100A10 and annexin A2.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Interactions

Background:

  • S100 proteins are calcium-binding proteins involved in various cellular processes.
  • Calcium binding induces conformational changes in S100 proteins, mediating interactions with diverse biological targets.
  • Previous studies elucidated S100 protein structures with peptide targets, revealing multiple recognition modes and distinct interaction surfaces.

Purpose of the Study:

  • To review potential multiprotein complexes involving calcium-insensitive S100A10.
  • To explore the interactions of S100A10 with annexin A2 and other associated proteins.
  • To highlight the significance of S100 protein structural dynamics in biological recognition.

Main Methods:

  • Analysis of existing three-dimensional structures of S100 proteins.
  • Examination of S100 protein interactions with known peptide targets.
  • Literature review focusing on multiprotein complex formation involving S100A10.

Main Results:

  • Calcium binding to S100 proteins (S100B, S100A1, S100A6, S100A11) induces conformational changes.
  • At least three distinct recognition modes utilize two surfaces on S100 proteins.
  • Hypothesized simultaneous accommodation of multiple binding partners on S100 protein surfaces.

Conclusions:

  • S100 proteins play a crucial role in mediating complex biological interactions.
  • The review focuses on multiprotein complexes involving calcium-insensitive S100A10, annexin A2, AHNAK, dysferlin, NS3, TASK-1, and TRPV5/6.
  • Understanding these complexes offers insights into cellular signaling and regulation.