1aym

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[[Category: site-directed mutagenesis]]
[[Category: site-directed mutagenesis]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 14:34:49 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 14:52:53 2007''

Revision as of 12:48, 30 October 2007


1aym, resolution 2.15Å

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HUMAN RHINOVIRUS 16 COAT PROTEIN AT HIGH RESOLUTION

Overview

BACKGROUND: Rhinoviruses belong to the picornavirus family and are small, icosahedral, non-enveloped viruses containing one positive RNA strand., Human rhinovirus 16 (HRV16) belongs to the major receptor group of, rhinoviruses, for which the cellular receptor is intercellular adhesion, molecule-1 (ICAM-1). In many rhinoviruses, one of the viral coat proteins, (VP1) contains a hydrophobic pocket which is occupied by a fatty acid-like, molecule, or so-called 'pocket factor'. Antiviral agents have been shown, to bind to the hydrophobic pocket in VP1, replacing the pocket factor. The, presence of the antiviral compound blocks uncoating of the virus and in, some cases inhibits receptor attachment. A refined, high-resolution, structure would be expected to provide further information on the ... [(full description)]

About this Structure

1AYM is a [Protein complex] structure of sequences from [Human rhinovirus sp.] with ZN, MYR and DAO as [ligands]. Structure known Active Sites: MYR, PO2, POC, RNA and ZN. Full crystallographic information is available from [OCA].

Reference

The refined structure of human rhinovirus 16 at 2.15 A resolution: implications for the viral life cycle., Hadfield AT, Lee W, Zhao R, Oliveira MA, Minor I, Rueckert RR, Rossmann MG, Structure. 1997 Mar 15;5(3):427-41. PMID:9083115

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