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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
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.
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.
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.