1irj
From Proteopedia
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Crystal Structure of the MRP14 complexed with CHAPS
Overview
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.
About this Structure
1IRJ is a Single protein structure of sequence from Homo sapiens with CA and CPS as ligands. Full crystallographic information is available from OCA.
Reference
The crystal structure of human MRP14 (S100A9), a Ca(2+)-dependent regulator protein in inflammatory process., Itou H, Yao M, Fujita I, Watanabe N, Suzuki M, Nishihira J, Tanaka I, J Mol Biol. 2002 Feb 15;316(2):265-76. PMID:11851337
Page seeded by OCA on Mon Nov 12 17:33:55 2007
Categories: Homo sapiens | Single protein | Itou, H. | Nishihira, J. | Tanaka, I. | Watanabe, N. | Yao, M. | CA | CPS | Calgranulin b | Ef-hand | Mrp14 | S100a9
