2fv5: Difference between revisions

Revision as of 19:48, 27 July 2008

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File:2fv5.png

Template:STRUCTURE 2fv5

Crystal structure of TACE in complex with IK682Crystal structure of TACE in complex with IK682

Template:ABSTRACT PUBMED 16762314

About this StructureAbout this Structure

2FV5 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

IK682, a tight binding inhibitor of TACE., Niu X, Umland S, Ingram R, Beyer BM, Liu YH, Sun J, Lundell D, Orth P, Arch Biochem Biophys. 2006 Jul 1;451(1):43-50. Epub 2006 May 5. PMID:16762314

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OCA

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-[[Image:2fv5.gif|left|200px]]
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 {{STRUCTURE_2fv5|  PDB=2fv5  |  SCENE=  }}
-'''Crystal structure of TACE in complex with IK682'''
+===Crystal structure of TACE in complex with IK682===
-==Overview==
+<!--
-TNFalpha converting enzyme (TACE) is the major metalloproteinase for the processing of TNFalpha, a key inflammatory cytokine. IK682, a hydroxamate compound, was reported to be a potent and specific TACE inhibitor [J.J. Duan, L. Chen, Z.R. Wasserman, Z. Lu, R.Q. Liu, M.B. Covington, M. Qian, K.D. Hardman, R.L. Magolda, R.C. Newton, D.D. Christ, R.R. Wexler, C.P. Decicco, J. Med. Chem. 45 (2002) 4954-4957]. The binding kinetics of IK682 and the ectodomain of human TACE was examined. The k(on) of IK682 was determined as 1.1+/-0.3 x 10(8) M(-1) min(-1). No detectable dissociation of IK682 from TACE was observed following dialysis, dilution, and extensive washing over a maximum of 72 h. This was in contrast to the rapid dissociation of IK682 from ADAM10. LC/MS analysis of the TACE-IK682 complex after dissociation under denaturing conditions indicated that the tight binding is not due to covalent interaction. The X-ray crystal structure of TACE-IK682 complex revealed multiple binding points at the S1' and S3' sites and the movement of a loop (from Ala349 to Gly442) to accommodate the binding of the quinolinyl group of IK682 at the S3' pocket. The conformational changes of TACE may contribute significantly to the high affinity binding as a result of a more stable TACE-inhibitor complex.
+The line below this paragraph, {{ABSTRACT_PUBMED_16762314}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16762314 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_16762314}}
 ==About this Structure==
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 [[Category: Orth, P.]]
 [[Category: Tace adam17 zn-endopeptidase]]
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