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Related Experiment Videos

The three-dimensional structure of human S100A12.

O V Moroz1, A A Antson, G N Murshudov

  • 1Structural Biology Laboratory, Department of Chemistry, University of York, York YO10 5DD, England.

Acta Crystallographica. Section D, Biological Crystallography
|January 3, 2001
PubMed
Summary

The crystal structure of human S100A12 protein reveals its calcium-bound dimer form. This provides insights into EF-hand calcium-binding proteins and their interactions, including potential roles in inflammation.

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Area of Science:

  • Structural biology
  • Biochemistry
  • Molecular biology

Background:

  • S100A12 is a human EF-hand calcium-binding protein.
  • S100 proteins are homologous to calmodulin and play roles in various cellular processes.
  • The specific function of S100A12 in cell behavior remains largely undefined.

Purpose of the Study:

  • To determine the crystal structure of human S100A12 in its calcium-bound form.
  • To compare the structure of S100A12 with other S100 family members.
  • To understand the structural basis for S100A12's interactions and potential functions.

Main Methods:

  • X-ray crystallography to determine the 3D structure.
  • Molecular replacement using the S100B protein structure.
  • Sequence and structure comparisons within the S100 protein family.

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Main Results:

  • The crystal structure of calcium-bound S100A12 was determined at 1.95 A resolution.
  • S100A12 forms a dimer with a hydrophobic interface, similar to other S100 proteins.
  • A unique linker region between EF-hand motifs was observed, potentially forming the target-binding site in conjunction with other residues.

Conclusions:

  • The determined structure provides a detailed molecular understanding of S100A12.
  • Structural comparisons highlight conserved residues and regions involved in inter-subunit interactions.
  • S100A12's interaction with the RAGE receptor suggests a role in inflammatory responses.