2cl5

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spinqualitylabelsall models 2cl5, resolution 1.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

CATECHOL-O-METHYLTRANSFERASE IN COMPLEX WITH AN INHIBITOR

Overview

In this work, we present a comparative case study of "ortho-" and, "meta-nitrated" catecholic inhibitors of catechol-O-methyltransferase, (COMT), with regard to their interaction with the catalytic site of the, enzyme and the in vitro regioselective formation of their mono-O-methyl, ether metabolites. In particular, the effects of altering the attachment, position of the inhibitors' side-chain substituent, within the classic, nitrocatechol pharmacophore, were investigated. For this purpose, we, compared two simple regioisomeric nitrocatechol-type inhibitors of COMT, BIA 3-228 and BIA 8-176, which contain the benzoyl substituent attached at, the meta and ortho positions, respectively, relative to the nitro group., The two compounds were slowly O-methylated by COMT in vitro, but the, ... [(full description)]

About this Structure

2CL5 is a [Single protein] structure of sequence from [Rattus norvegicus] with MG, SAM, BIE, BU3 and MES as [ligands]. Active as [Catechol O-methyltransferase], with EC number [2.1.1.6]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

Comparative study of ortho- and meta-nitrated inhibitors of catechol-O-methyltransferase: interactions with the active site and regioselectivity of O-methylation., Palma PN, Rodrigues ML, Archer M, Bonifacio MJ, Loureiro AI, Learmonth DA, Carrondo MA, Soares-da-Silva P, Mol Pharmacol. 2006 Jul;70(1):143-53. Epub 2006 Apr 17. PMID:16618795

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