1irj: Difference between revisions

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[[Image:1irj.gif|left|200px]]
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[[Image:1irj.png|left|200px]]


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{{STRUCTURE_1irj|  PDB=1irj  |  SCENE=  }}  
{{STRUCTURE_1irj|  PDB=1irj  |  SCENE=  }}  


'''Crystal Structure of the MRP14 complexed with CHAPS'''
===Crystal Structure of the MRP14 complexed with CHAPS===




==Overview==
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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.
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{{ABSTRACT_PUBMED_11851337}}


==About this Structure==
==About this Structure==
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[[Category: Mrp14]]
[[Category: Mrp14]]
[[Category: S100a9]]
[[Category: S100a9]]
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Revision as of 13:52, 1 July 2008

File:1irj.png

Template:STRUCTURE 1irj

Crystal Structure of the MRP14 complexed with CHAPSCrystal Structure of the MRP14 complexed with CHAPS

Template:ABSTRACT PUBMED 11851337

About this StructureAbout this Structure

1IRJ is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

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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