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Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
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Mapping Dysfunctional Protein-Protein Interactions in Disease
09:39

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Published on: October 24, 2025

S100A11: diverse function and pathology corresponding to different target proteins.

Honglin He1, Jingjing Li, Shunyan Weng

  • 1Shanghai Municipality Key Laboratory of Veterinary Biotechnology, School of Agriculture and Biology, Shanghai Jiao Tong University, Shanghai, 200240, People's Republic of China.

Cell Biochemistry and Biophysics
|August 4, 2009
PubMed
Summary

S100A11 protein, a calcium-binding molecule, plays diverse roles in inflammation and cell growth. It can act as both a tumor suppressor and promoter, influencing cancer cell proliferation.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • S100A11 is a member of the S100 protein family, characterized by EF-hand calcium-binding domains.
  • It exhibits unique characteristics despite sharing common features with other EF-hand calcium-binding proteins.
  • S100A11 is broadly expressed across tissues and localized in the cytoplasm, nucleus, and cell periphery.

Purpose of the Study:

  • To systematically describe the biological roles of S100A11.
  • To elucidate the mechanisms by which S100A11 interacts with target proteins.
  • To explore the involvement of S100A11 in inflammation, enzyme activity regulation, and cell growth.

Main Methods:

  • Review and systematic description of existing literature on S100A11.
  • Analysis of S100A11's interactions with various target proteins.
  • Investigation of S100A11's conformational changes upon calcium binding.

Main Results:

  • S100A11 exists as a non-covalent homodimer with an antiparallel conformation.
  • Calcium binding induces conformational changes, exposing a hydrophobic cleft for target protein interaction.
  • S100A11 functions as a dual mediator of cell growth, acting as a tumor suppressor or promoter in different cancers.

Conclusions:

  • S100A11 exhibits diverse biological functions, including roles in inflammation and cell growth regulation.
  • Its dual role as a tumor suppressor or promoter highlights its complex involvement in cancer.
  • Further research on S100A11 is crucial for a comprehensive understanding of its biological significance.