1nhv: Difference between revisions

Revision as of 13:15, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1nhv.png

Template:STRUCTURE 1nhv

Hepatitis C virus RNA polymerase in complex with non-nucleoside analogue inhibitorHepatitis C virus RNA polymerase in complex with non-nucleoside analogue inhibitor

Template:ABSTRACT PUBMED 12509436

About this StructureAbout this Structure

1NHV is a Single protein structure of sequence from Hepatitis c virus. Full crystallographic information is available from OCA.

ReferenceReference

Non-nucleoside analogue inhibitors bind to an allosteric site on HCV NS5B polymerase. Crystal structures and mechanism of inhibition., Wang M, Ng KK, Cherney MM, Chan L, Yannopoulos CG, Bedard J, Morin N, Nguyen-Ba N, Alaoui-Ismaili MH, Bethell RC, James MN, J Biol Chem. 2003 Mar 14;278(11):9489-95. Epub 2002 Dec 30. PMID:12509436

Page seeded by OCA on Tue Jul 29 13:15:26 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Hepatitis C virus RNA polymerase in complex with non-nucleoside analogue inhibitor'''
+===Hepatitis C virus RNA polymerase in complex with non-nucleoside analogue inhibitor===
-==Overview==
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-X-ray crystal structures of two non-nucleoside analogue inhibitors bound to hepatitis C virus NS5B RNA-dependent RNA polymerase have been determined to 2.0 and 2.9 A resolution. These noncompetitive inhibitors bind to the same site on the protein, approximately 35 A from the active site. The common features of binding include a large hydrophobic region and two hydrogen bonds between both oxygen atoms of a carboxylate group on the inhibitor and two main chain amide nitrogen atoms of Ser(476) and Tyr(477) on NS5B. The inhibitor-binding site lies at the base of the thumb domain, near its interface with the C-terminal extension of NS5B. The location of this inhibitor-binding site suggests that the binding of these inhibitors interferes with a conformational change essential for the activity of the polymerase.
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 [[Category: Rna polymerase]]
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