1zvx: Difference between revisions

Revision as of 07:53, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1zvx.png

Template:STRUCTURE 1zvx

Crystal structure of the complex between MMP-8 and a phosphonate inhibitor (R-enantiomer)Crystal structure of the complex between MMP-8 and a phosphonate inhibitor (R-enantiomer)

Template:ABSTRACT PUBMED 16451058

About this StructureAbout this Structure

1ZVX is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Structural insight into the stereoselective inhibition of MMP-8 by enantiomeric sulfonamide phosphonates., Pochetti G, Gavuzzo E, Campestre C, Agamennone M, Tortorella P, Consalvi V, Gallina C, Hiller O, Tschesche H, Tucker PA, Mazza F, J Med Chem. 2006 Feb 9;49(3):923-31. PMID:16451058

X-ray structure of human stromelysin catalytic domain complexed with nonpeptide inhibitors: implications for inhibitor selectivity., Pavlovsky AG, Williams MG, Ye QZ, Ortwine DF, Purchase CF 2nd, White AD, Dhanaraj V, Roth BD, Johnson LL, Hupe D, Humblet C, Blundell TL, Protein Sci. 1999 Jul;8(7):1455-62. PMID:10422833

Two crystal structures of human neutrophil collagenase, one complexed with a primed- and the other with an unprimed-side inhibitor: implications for drug design., Gavuzzo E, Pochetti G, Mazza F, Gallina C, Gorini B, D'Alessio S, Pieper M, Tschesche H, Tucker PA, J Med Chem. 2000 Sep 7;43(18):3377-85. PMID:10978185

X-ray structures of human neutrophil collagenase complexed with peptide hydroxamate and peptide thiol inhibitors. Implications for substrate binding and rational drug design., Grams F, Reinemer P, Powers JC, Kleine T, Pieper M, Tschesche H, Huber R, Bode W, Eur J Biochem. 1995 Mar 15;228(3):830-41. PMID:7737183

Page seeded by OCA on Tue Jul 29 07:53:04 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:1zvx.gif|left|200px]]
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 {{STRUCTURE_1zvx|  PDB=1zvx  |  SCENE=  }}
-'''Crystal structure of the complex between MMP-8 and a phosphonate inhibitor (R-enantiomer)'''
+===Crystal structure of the complex between MMP-8 and a phosphonate inhibitor (R-enantiomer)===
-==Overview==
+<!--
-Potent and selective inhibitors of matrix metalloproteinases (MMPs), a family of zinc proteases that can degrade all the components of the extracellular matrix, could be useful for treatment of diseases such as cancer and arthritis. The most potent MMP inhibitors are based on hydroxamate as zinc-binding group (ZBG). alpha-Arylsulfonylamino phosphonates incorporate a particularly favorable combination of phosphonate as ZBG and arylsulfonylamino backbone so that their affinity exceptionally attains the nanomolar strength frequently observed for hydroxamate analogues. The detailed mode of binding of [1-(4'-methoxybiphenyl-4-sulfonylamino)-2-methylpropyl]phosphonate has been clarified by the crystal structures of the complexes that the R- and S-enantiomers respectively form with MMP-8. The reasons for the preferential MMP-8 inhibition by the R-phosphonate are underlined and the differences in the mode of binding of analogous alpha-arylsulfonylamino hydroxamates and carboxylates are discussed.
+The line below this paragraph, {{ABSTRACT_PUBMED_16451058}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16451058 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_16451058}}
 ==About this Structure==
@@ Line 20: / Line 24: @@
 ==Reference==
 Structural insight into the stereoselective inhibition of MMP-8 by enantiomeric sulfonamide phosphonates., Pochetti G, Gavuzzo E, Campestre C, Agamennone M, Tortorella P, Consalvi V, Gallina C, Hiller O, Tschesche H, Tucker PA, Mazza F, J Med Chem. 2006 Feb 9;49(3):923-31. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16451058 16451058]
+X-ray structure of human stromelysin catalytic domain complexed with nonpeptide inhibitors: implications for inhibitor selectivity., Pavlovsky AG, Williams MG, Ye QZ, Ortwine DF, Purchase CF 2nd, White AD, Dhanaraj V, Roth BD, Johnson LL, Hupe D, Humblet C, Blundell TL, Protein Sci. 1999 Jul;8(7):1455-62. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10422833 10422833]
+Two crystal structures of human neutrophil collagenase, one complexed with a primed- and the other with an unprimed-side inhibitor: implications for drug design., Gavuzzo E, Pochetti G, Mazza F, Gallina C, Gorini B, D'Alessio S, Pieper M, Tschesche H, Tucker PA, J Med Chem. 2000 Sep 7;43(18):3377-85. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10978185 10978185]
+X-ray structures of human neutrophil collagenase complexed with peptide hydroxamate and peptide thiol inhibitors. Implications for substrate binding and rational drug design., Grams F, Reinemer P, Powers JC, Kleine T, Pieper M, Tschesche H, Huber R, Bode W, Eur J Biochem. 1995 Mar 15;228(3):830-41. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7737183 7737183]
 [[Category: Homo sapiens]]
 [[Category: Neutrophil collagenase]]
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 [[Category: Stereoselective inhibition]]
 [[Category: Sulfonamide junction]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 18:08:36 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 07:53:04 2008''