2rjp

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|PDB= 2rjp |SIZE=350|CAPTION= <scene name='initialview01'>2rjp</scene>, resolution 2.800&Aring;
|PDB= 2rjp |SIZE=350|CAPTION= <scene name='initialview01'>2rjp</scene>, resolution 2.800&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=886:N-({4'-[(4-isobutyrylphenoxy)methyl]biphenyl-4-yl}sulfonyl)-D-valine'>886</scene>
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|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=886:N-({4&#39;-[(4-isobutyrylphenoxy)methyl]biphenyl-4-yl}sulfonyl)-D-valine'>886</scene>
|ACTIVITY= [http://en.wikipedia.org/wiki/ADAMTS-4_endopeptidase ADAMTS-4 endopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.82 3.4.24.82]
|ACTIVITY= [http://en.wikipedia.org/wiki/ADAMTS-4_endopeptidase ADAMTS-4 endopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.82 3.4.24.82]
|GENE= ADAMTS4, KIAA0688 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
|GENE= ADAMTS4, KIAA0688 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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[[Category: zymogen]]
[[Category: zymogen]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:36:49 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 15:49:55 2008''

Revision as of 13:49, 23 March 2008

Image:2rjp.jpg


PDB ID 2rjp

Drag the structure with the mouse to rotate
, resolution 2.800Å
Ligands: , and
Gene: ADAMTS4, KIAA0688 (Homo sapiens)
Activity: ADAMTS-4 endopeptidase, with EC number 3.4.24.82
Coordinates: save as pdb, mmCIF, xml



Crystal structure of ADAMTS4 with inhibitor bound


Overview

Aggrecanases are now believed to be the principal proteinases responsible for aggrecan degradation in osteoarthritis. Given their potential as a drug target, we solved crystal structures of the two most active human aggrecanase isoforms, ADAMTS4 and ADAMTS5, each in complex with bound inhibitor and one wherein the enzyme is in apo form. These structures show that the unliganded and inhibitor-bound enzymes exhibit two essentially different catalytic-site configurations: an autoinhibited, nonbinding, closed form and an open, binding form. On this basis, we propose that mature aggrecanases exist as an ensemble of at least two isomers, only one of which is proteolytically active.

About this Structure

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

Reference

Crystal structures of the two major aggrecan degrading enzymes, ADAMTS4 and ADAMTS5., Mosyak L, Georgiadis K, Shane T, Svenson K, Hebert T, McDonagh T, Mackie S, Olland S, Lin L, Zhong X, Kriz R, Reifenberg EL, Collins-Racie LA, Corcoran C, Freeman B, Zollner R, Marvell T, Vera M, Sum PE, Lavallie ER, Stahl M, Somers W, Protein Sci. 2008 Jan;17(1):16-21. Epub 2007 Nov 27. PMID:18042673

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