1dxw: Difference between revisions
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Revision as of 15:57, 30 October 2007
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STRUCTURE OF HETERO COMPLEX OF NON STRUCTURAL PROTEIN (NS) OF HEPATITIS C VIRUS (HCV) AND SYNTHETIC PEPTIDIC COMPOUND
OverviewOverview
Few structures of viral serine proteases, those encoded by the Sindbis and, Semliki Forest viruses, hepatitis C virus (HCV) and cytomegalovirus, have, been reported. In the life cycle of HCV a crucial role is played by a, chymotrypsin-like serine protease encoded at the N-terminus of the viral, NS3 protein, the solution structure of which we present here complexed, with a covalently bound reversible inhibitor. Unexpectedly, the residue in, the P2 position of the inhibitor induces an effective stabilization of the, catalytic His-Asp hydrogen bond, by shielding that region of the protease, from the solvent. This interaction appears crucial in the activation of, the enzyme catalytic machinery and represents an unprecedented observation, for this family of enzymes. Our data suggest that ... [(full description)]
About this StructureAbout this Structure
1DXW is a [Single protein] structure of sequence from [Viruses] with ZN as [ligand]. Structure known Active Sites: CAT and ZNB. Full crystallographic information is available from [OCA].
ReferenceReference
Inhibitor binding induces active site stabilization of the HCV NS3 protein serine protease domain., Barbato G, Cicero DO, Cordier F, Narjes F, Gerlach B, Sambucini S, Grzesiek S, Matassa VG, De Francesco R, Bazzo R, EMBO J. 2000 Mar 15;19(6):1195-206. PMID:10716920
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