2ces: Difference between revisions

Revision as of 04:24, 29 July 2008

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File:2ces.png

Template:STRUCTURE 2ces

BETA-GLUCOSIDASE FROM THERMOTOGA MARITIMA IN COMPLEX WITH GLUCOIMIDAZOLEBETA-GLUCOSIDASE FROM THERMOTOGA MARITIMA IN COMPLEX WITH GLUCOIMIDAZOLE

Template:ABSTRACT PUBMED 17002288

About this StructureAbout this Structure

2CES is a Single protein structure of sequence from Thermotoga maritima. Full crystallographic information is available from OCA.

ReferenceReference

Structural, kinetic, and thermodynamic analysis of glucoimidazole-derived glycosidase inhibitors., Gloster TM, Roberts S, Perugino G, Rossi M, Moracci M, Panday N, Terinek M, Vasella A, Davies GJ, Biochemistry. 2006 Oct 3;45(39):11879-84. PMID:17002288

Page seeded by OCA on Tue Jul 29 04:24:05 2008

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OCA

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-'''BETA-GLUCOSIDASE FROM THERMOTOGA MARITIMA IN COMPLEX WITH GLUCOIMIDAZOLE'''
+===BETA-GLUCOSIDASE FROM THERMOTOGA MARITIMA IN COMPLEX WITH GLUCOIMIDAZOLE===
-==Overview==
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-Inhibition of glycosidases has great potential in the quest for highly potent and specific drugs to treat diseases such as diabetes, cancer, and viral infections. One of the most effective ways of designing such compounds is by mimicking the transition state. Here we describe the structural, kinetic, and thermodynamic dissection of binding of two glucoimidazole-derived compounds, which are among the most potent glycosidase inhibitors reported to date, with two family 1 beta-glycosidases. Provocatively, while inclusion of the phenethyl moiety improves binding by a factor of 20-80-fold, this does not appear to result from better noncovalent interactions with the enzyme; instead, improved affinity may be derived from significantly better entropic contributions to binding displayed by the phenethyl-substituted imidazole compound.
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