1irj: Difference between revisions

New page: left|200px<br /> <applet load="1irj" size="450" color="white" frame="true" align="right" spinBox="true" caption="1irj, resolution 2.10Å" /> '''Crystal Structure o...
 
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[[Image:1irj.gif|left|200px]]<br />
[[Image:1irj.gif|left|200px]]<br /><applet load="1irj" size="350" color="white" frame="true" align="right" spinBox="true"  
<applet load="1irj" size="450" color="white" frame="true" align="right" spinBox="true"  
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==
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.
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==
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].  
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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