1dxw: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1dxw.gif|left|200px]] | [[Image:1dxw.gif|left|200px]] | ||
<!-- | |||
The line below this paragraph, containing "STRUCTURE_1dxw", creates the "Structure Box" on the page. | |||
You may change the PDB parameter (which sets the PDB file loaded into the applet) | |||
or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |||
| | or leave the SCENE parameter empty for the default display. | ||
| | --> | ||
{{STRUCTURE_1dxw| PDB=1dxw | SCENE= }} | |||
}} | |||
'''STRUCTURE OF HETERO COMPLEX OF NON STRUCTURAL PROTEIN (NS) OF HEPATITIS C VIRUS (HCV) AND SYNTHETIC PEPTIDIC COMPOUND''' | '''STRUCTURE OF HETERO COMPLEX OF NON STRUCTURAL PROTEIN (NS) OF HEPATITIS C VIRUS (HCV) AND SYNTHETIC PEPTIDIC COMPOUND''' | ||
| Line 35: | Line 32: | ||
[[Category: Narjes, F.]] | [[Category: Narjes, F.]] | ||
[[Category: Sambucini, S.]] | [[Category: Sambucini, S.]] | ||
[[Category: | [[Category: Hepatitis c virus]] | ||
[[Category: | [[Category: Hydrolase]] | ||
[[Category: | [[Category: Non structural protein]] | ||
[[Category: | [[Category: Serine protease]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:24:53 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | |||
Revision as of 14:24, 2 May 2008
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 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 StructureAbout this Structure
1DXW is a Single protein structure of sequence from Viruses. 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 Page seeded by OCA on Fri May 2 14:24:53 2008