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1irj

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(New page: 200px<br /> <applet load="1irj" size="450" color="white" frame="true" align="right" spinBox="true" caption="1irj, resolution 2.10&Aring;" /> '''Crystal Structure o...)
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Revision as of 15:27, 12 November 2007

Image:1irj.gif

1irj, resolution 2.10Å

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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

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