The crystal structure of human MRP14 (S100A9), a Ca(2+)-dependent regulator protein in inflammatory process.

Human MRP14 (hMRP14) is a Ca(2+)-binding protein from the S100 family of proteins. This protein is co-expressed with human MRP8 (hMRP8), a homologue protein in myeloid cells, and plays an indispensable role in Ca(2+)-dependent functions during inflammation. This role includes the activation of Mac-1, the beta(2) integrin which is involved ...
in neutrophil adhesion to endothelial cells. The crystal structure of the holo form of hMRP14 was analyzed at 2.1 A resolution. hMRP14 is distinguished from other S100 member proteins by its long C-terminal region, and its structure shows that the region is extensively flexible. In this crystal structure of hMRP14, Chaps molecules bind to the hinge region that connects two EF-hand motifs, which suggests that this region is a target-binding site of this protein. Based on a structural comparison of hMRP14 with hMRP8 and human S100A12 (hS100A12) that is another homologue protein, the character of MRP8/14 hetero-complex and the functional significance of the flexibility of the C-terminal region of hMRP14 are discussed.
Mesh Terms:
Amino Acid Sequence, Antigens, Differentiation, Binding Sites, Calcium, Calgranulin B, Crystallography, X-Ray, Dimerization, EF Hand Motifs, Humans, Hydrophobicity, Inflammation, Leukocyte L1 Antigen Complex, Membrane Glycoproteins, Models, Molecular, Molecular Sequence Data, Molecular Weight, Neural Cell Adhesion Molecules, Pliability, Protein Structure, Quaternary, Protein Structure, Secondary, S100 Proteins, Sequence Alignment, Static Electricity
J. Mol. Biol.
Date: Feb. 15, 2002
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