2imb: Difference between revisions

Revision as of 12:50, 28 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:2imb.png

Template:STRUCTURE 2imb

Clostridium botulinum Neurotoxin Serotype A Light Chain Inhibited by L-arginine hydroxamateClostridium botulinum Neurotoxin Serotype A Light Chain Inhibited by L-arginine hydroxamate

Template:ABSTRACT PUBMED 17524984

About this StructureAbout this Structure

2IMB is a Single protein structure of sequence from Clostridium botulinum. Full crystallographic information is available from OCA.

ReferenceReference

Structures of Clostridium botulinum Neurotoxin Serotype A Light Chain complexed with small-molecule inhibitors highlight active-site flexibility., Silvaggi NR, Boldt GE, Hixon MS, Kennedy JP, Tzipori S, Janda KD, Allen KN, Chem Biol. 2007 May;14(5):533-42. PMID:17524984

Page seeded by OCA on Mon Jul 28 12:50:47 2008

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

OCA

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-'''Clostridium botulinum Neurotoxin Serotype A Light Chain Inhibited by L-arginine hydroxamate'''
+===Clostridium botulinum Neurotoxin Serotype A Light Chain Inhibited by L-arginine hydroxamate===
-==Overview==
+<!--
-The potential for the use of Clostridial neurotoxins as bioweapons makes the development of small-molecule inhibitors of these deadly toxins a top priority. Recently, screening of a random hydroxamate library identified a small-molecule inhibitor of C. botulinum Neurotoxin Serotype A Light Chain (BoNT/A-LC), 4-chlorocinnamic hydroxamate, a derivative of which has been shown to have in vivo efficacy in mice and no toxicity. We describe the X-ray crystal structures of BoNT/A-LC in complexes with two potent small-molecule inhibitors. The structures of the enzyme with 4-chlorocinnamic hydroxamate or 2,4-dichlorocinnamic hydroxamate bound are compared to the structure of the enzyme complexed with L-arginine hydroxamate, an inhibitor with modest affinity. Taken together, this suite of structures provides surprising insights into the BoNT/A-LC active site, including unexpected conformational flexibility at the S1' site that changes the electrostatic environment of the binding pocket. Information gained from these structures will inform the design and optimization of more effective small-molecule inhibitors of BoNT/A-LC.
+The line below this paragraph, {{ABSTRACT_PUBMED_17524984}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_17524984}}
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