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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[[Image:1irj.gif|left|200px]]<br />
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[[Image:1irj.gif|left|200px]]<br /><applet load="1irj" size="350" color="white" frame="true" align="right" spinBox="true"
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<applet load="1irj" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1irj, resolution 2.10&Aring;" />
caption="1irj, resolution 2.10&Aring;" />
'''Crystal Structure of the MRP14 complexed with CHAPS'''<br />
'''Crystal Structure of the MRP14 complexed with CHAPS'''<br />
==Overview==
==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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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==
==About this Structure==
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1IRJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with CA and CPS as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1IRJ OCA].
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1IRJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=CPS:'>CPS</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IRJ OCA].
==Reference==
==Reference==
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[[Category: s100a9]]
[[Category: s100a9]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:33:55 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:14:50 2008''

Revision as of 11:14, 21 February 2008


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 and 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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