1dxw
From Proteopedia
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| - | [[Image:1dxw.gif|left|200px]]<br /> | + | [[Image:1dxw.gif|left|200px]]<br /><applet load="1dxw" size="450" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1dxw" size="450" color="white" frame="true" align="right" spinBox="true" | + | |
caption="1dxw" /> | caption="1dxw" /> | ||
'''STRUCTURE OF HETERO COMPLEX OF NON STRUCTURAL PROTEIN (NS) OF HEPATITIS C VIRUS (HCV) AND SYNTHETIC PEPTIDIC COMPOUND'''<br /> | '''STRUCTURE OF HETERO COMPLEX OF NON STRUCTURAL PROTEIN (NS) OF HEPATITIS C VIRUS (HCV) AND SYNTHETIC PEPTIDIC COMPOUND'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1DXW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Viruses Viruses] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. | + | 1DXW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Viruses Viruses] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Sites: <scene name='pdbsite=CAT:The Catalytic Triad Is Formed By Residues SER 139, HIS 5 ...'>CAT</scene> and <scene name='pdbsite=ZNB:Zn Binding Site, The HIS Is Bound Through A Water Molecu ...'>ZNB</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DXW OCA]. |
==Reference== | ==Reference== | ||
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[[Category: serine protease]] | [[Category: serine protease]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 14:46:48 2007'' |
Revision as of 12:37, 18 December 2007
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STRUCTURE OF HETERO COMPLEX OF NON STRUCTURAL PROTEIN (NS) OF HEPATITIS C VIRUS (HCV) AND SYNTHETIC PEPTIDIC COMPOUND
Overview
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 natural substrates of, this serine protease could contribute to the enzyme activation by a, similar induced-fit mechanism. The high degree of similarity at the, His-Asp catalytic site region between HCV NS3 and other viral serine, proteases suggests that this behaviour could be a more general feature for, this category of viral enzymes.
About this Structure
1DXW is a Single protein structure of sequence from Viruses with ZN as ligand. Known structural/functional Sites: and . Full crystallographic information is available from OCA.
Reference
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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