1w75

From Proteopedia

Revision as of 12:14, 30 October 2007

NATIVE ORTHORHOMBIC FORM OF TORPEDO CALIFORNICA ACETYLCHOLINESTERASE (ACHE)

Overview

Bifunctional derivatives of the alkaloid galanthamine, designed to, interact with both the active site of the enzyme acetylcholinesterase, (AChE) and its peripheral cation binding site, have been assayed with, Torpedo californica AChE (TcAChE), and the three-dimensional structures of, their complexes with the enzyme have been solved by X-ray crystallography., Differences were noted between the IC(50) values obtained for TcAChE and, those for Electrophorus electricus AChE. These differences are ascribed to, sequence differences in one or two residues lining the active-site gorge, of the enzyme. The binding of one of the inhibitors disrupts the native, conformation of one wall of the gorge, formed by the loop Trp279-Phe290., It is proposed that flexibility of this loop may permit the ... [(full description)]

About this Structure

1W75 is a [Single protein] structure of sequence from [Torpedo californica] with NAG as [ligand]. Active as [Acetylcholinesterase], with EC number [3.1.1.7]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

The complex of a bivalent derivative of galanthamine with torpedo acetylcholinesterase displays drastic deformation of the active-site gorge: implications for structure-based drug design., Greenblatt HM, Guillou C, Guenard D, Argaman A, Botti S, Badet B, Thal C, Silman I, Sussman JL, J Am Chem Soc. 2004 Dec 1;126(47):15405-11. PMID:15563167

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