2ouc

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[[Image:2ouc.jpg|left|200px]]
[[Image:2ouc.jpg|left|200px]]
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{{Structure
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|PDB= 2ouc |SIZE=350|CAPTION= <scene name='initialview01'>2ouc</scene>, resolution 2.20&Aring;
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The line below this paragraph, containing "STRUCTURE_2ouc", creates the "Structure Box" on the page.
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|GENE= MKP5 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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{{STRUCTURE_2ouc| PDB=2ouc | SCENE= }}
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|RELATEDENTRY=[[2oud|2OUD]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ouc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ouc OCA], [http://www.ebi.ac.uk/pdbsum/2ouc PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2ouc RCSB]</span>
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'''Crystal structure of the MAP kinase binding domain of MKP5'''
'''Crystal structure of the MAP kinase binding domain of MKP5'''
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[[Category: Tao, X.]]
[[Category: Tao, X.]]
[[Category: Tong, L.]]
[[Category: Tong, L.]]
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[[Category: hydrolase]]
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[[Category: Hydrolase]]
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[[Category: rhodanese fold]]
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[[Category: Rhodanese fold]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 11:40:28 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:23:13 2008''
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Revision as of 08:40, 4 May 2008

Image:2ouc.jpg

Template:STRUCTURE 2ouc

Crystal structure of the MAP kinase binding domain of MKP5


Overview

MAP kinase phosphatases (MKPs) have crucial roles in regulating the signaling activity of MAP kinases and are potential targets for drug discovery against human diseases. These enzymes contain a catalytic domain (CD) as well as a binding domain (BD) that help recognize the target MAP kinase. We report here the crystal structures at up to 2.2 A resolution of the BD and CD of human MKP5 and compare them to the known structures from other MKPs. Dramatic structural differences are observed between the BD of MKP5 and that of MKP3 determined previously by NMR. In particular, the cluster of positively charged residues that is important for MAP kinase binding is located in completely different positions in the two structures, with a distance of 25 A between them. Moreover, this cluster is alpha-helical in MKP5, while it forms a loop followed by a beta-strand in MKP3. These large structural differences could be associated with the distinct substrate preferences of these phosphatases, but further studies are needed to confirm this. The CD of MKP5 is observed in an active conformation, and two loops in the active site have backbone shifts of up to 5 A relative to the inactive CDs from other MKPs.

About this Structure

2OUC is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structure of the MAP kinase binding domain and the catalytic domain of human MKP5., Tao X, Tong L, Protein Sci. 2007 May;16(5):880-6. Epub 2007 Mar 30. PMID:17400920 Page seeded by OCA on Sun May 4 11:40:28 2008

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