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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
2002-3-7
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pubmed:databankReference |
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pubmed:abstractText |
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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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0022-2836
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pubmed:author |
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pubmed:copyrightInfo |
Copyright 2002 Academic Press.
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
316
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
265-76
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:11851337-Amino Acid Sequence,
pubmed-meshheading:11851337-Antigens, Differentiation,
pubmed-meshheading:11851337-Binding Sites,
pubmed-meshheading:11851337-Calcium,
pubmed-meshheading:11851337-Calgranulin B,
pubmed-meshheading:11851337-Crystallography, X-Ray,
pubmed-meshheading:11851337-Dimerization,
pubmed-meshheading:11851337-EF Hand Motifs,
pubmed-meshheading:11851337-Humans,
pubmed-meshheading:11851337-Hydrophobic and Hydrophilic Interactions,
pubmed-meshheading:11851337-Inflammation,
pubmed-meshheading:11851337-Leukocyte L1 Antigen Complex,
pubmed-meshheading:11851337-Membrane Glycoproteins,
pubmed-meshheading:11851337-Models, Molecular,
pubmed-meshheading:11851337-Molecular Sequence Data,
pubmed-meshheading:11851337-Molecular Weight,
pubmed-meshheading:11851337-Neural Cell Adhesion Molecules,
pubmed-meshheading:11851337-Pliability,
pubmed-meshheading:11851337-Protein Structure, Quaternary,
pubmed-meshheading:11851337-Protein Structure, Secondary,
pubmed-meshheading:11851337-S100 Proteins,
pubmed-meshheading:11851337-Sequence Alignment,
pubmed-meshheading:11851337-Static Electricity
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pubmed:year |
2002
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pubmed:articleTitle |
The crystal structure of human MRP14 (S100A9), a Ca(2+)-dependent regulator protein in inflammatory process.
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pubmed:affiliation |
Division of Biological Sciences, Graduate School of Science, Hokkaido University, Sapporo 060-0810, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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