1a4g

From Proteopedia

Revision as of 12:40, 30 October 2007

INFLUENZA VIRUS B/BEIJING/1/87 NEURAMINIDASE COMPLEXED WITH ZANAMIVIR

Overview

The first paper in this series (see previous article) described, structure-activity studies of carboxamide analogues of zanamivir binding, to influenza virus sialidase types A and B and showed that inhibitory, activity of these compounds was much greater against influenza A enzyme., To understand the large differences in affinities, a number of, protein-ligand complexes have been investigated using crystallography and, molecular dynamics. The crystallographic studies show that the binding of, ligands containing tertiary amide groups is accompanied by the formation, of an intramolecular planar salt bridge between two amino acid residues in, the active site of the enzyme. It is proposed that the unexpected strong, binding of these inhibitors is a result of the burial of hydrophobic, surface ... [(full description)]

About this Structure

1A4G is a [Single protein] structure of sequence from [Influenza b virus] with NAG, CA and ZMR as [ligands]. Active as [Exo-alpha-sialidase], with EC number [3.2.1.18]. Structure known Active Sites: CHA, CHB, CLA, CLB, ZAA and ZAB. Full crystallographic information is available from [OCA].

Reference

Dihydropyrancarboxamides related to zanamivir: a new series of inhibitors of influenza virus sialidases. 2. Crystallographic and molecular modeling study of complexes of 4-amino-4H-pyran-6-carboxamides and sialidase from influenza virus types A and B., Taylor NR, Cleasby A, Singh O, Skarzynski T, Wonacott AJ, Smith PW, Sollis SL, Howes PD, Cherry PC, Bethell R, Colman P, Varghese J, J Med Chem. 1998 Mar 12;41(6):798-807. PMID:9526556

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