1a86: Difference between revisions

Revision as of 16:21, 30 June 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:1a86.png

Template:STRUCTURE 1a86

MMP8 WITH MALONIC AND ASPARTIC ACID BASED INHIBITORMMP8 WITH MALONIC AND ASPARTIC ACID BASED INHIBITOR

Template:ABSTRACT PUBMED 9655333

About this StructureAbout this Structure

1A86 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Structure of malonic acid-based inhibitors bound to human neutrophil collagenase. A new binding mode explains apparently anomalous data., Brandstetter H, Engh RA, Von Roedern EG, Moroder L, Huber R, Bode W, Grams F, Protein Sci. 1998 Jun;7(6):1303-9. PMID:9655333

Page seeded by OCA on Mon Jun 30 16:21:02 2008

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

OCA

@@ Line 1: / Line 1: @@
-[[Image:1a86.gif|left|200px]]
+{{Seed}}
+[[Image:1a86.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1a86|  PDB=1a86  |  SCENE=  }}
-'''MMP8 WITH MALONIC AND ASPARTIC ACID BASED INHIBITOR'''
+===MMP8 WITH MALONIC AND ASPARTIC ACID BASED INHIBITOR===
-==Overview==
+<!--
-Matrix metalloproteinases (MMPs) are a family of zinc endopeptidases, which have been implicated in various disease processes. Various classes of MMP inhibitors, including hydroxamic acids, phosphinic acids, and thiols, have been previously described. Most of these mimic peptides, and most likely bind analogous to the corresponding peptide substrates. Among the hydroxamic acids, malonic acid derivatives have been used as MMP inhibitors, although optimization of their inhibition potency was not successful. Here we report the design of malonic acid-based inhibitors using the X-ray structure of a collagenase/inhibitor complex, which revealed a nonsubstrate-like binding mode. The proposed beta-type turn-like conformation for the improved inhibitors was confirmed by X-ray crystallography. The observation of nonsubstrate-like binding confirms the original strategy for structure-based modeling of improved malonic acid inhibitors, and explains kinetic data that are inconsistent with substrate-like binding. Detailed interactions for the improved inhibitors seen in the crystal structure also suggest possibilities for further modifications in cycles of structure based drug design. Indeed, we have designed nonpeptidic inhibitors with approximately 500-fold improved inhibition based on these structures.
+The line below this paragraph, {{ABSTRACT_PUBMED_9655333}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 9655333 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_9655333}}
 ==About this Structure==
@@ Line 31: / Line 35: @@
 [[Category: Matrix metalloproteinase]]
 [[Category: Mmp8]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 09:57:36 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 16:21:02 2008''