2cet
From Proteopedia
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BETA-GLUCOSIDASE FROM THERMOTOGA MARITIMA IN COMPLEX WITH PHENETHYL-SUBSTITUTED GLUCOIMIDAZOLE
Overview
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.
About this Structure
2CET is a Single protein structure of sequence from Thermotoga maritima with , and as ligands. Active as Beta-glucosidase, with EC number 3.2.1.21 Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
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
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