2hd0
From Proteopedia
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|PDB= 2hd0 |SIZE=350|CAPTION= <scene name='initialview01'>2hd0</scene>, resolution 2.28Å | |PDB= 2hd0 |SIZE=350|CAPTION= <scene name='initialview01'>2hd0</scene>, resolution 2.28Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=BOG:B-OCTYLGLUCOSIDE'>BOG</scene>, <scene name='pdbligand=DMU:DECYL-BETA-D-MALTOPYRANOSIDE'>DMU</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2hd0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hd0 OCA], [http://www.ebi.ac.uk/pdbsum/2hd0 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2hd0 RCSB]</span> | ||
}} | }} | ||
| Line 25: | Line 28: | ||
[[Category: Marcotrigiano, J.]] | [[Category: Marcotrigiano, J.]] | ||
[[Category: Rice, C M.]] | [[Category: Rice, C M.]] | ||
| - | [[Category: BOG]] | ||
| - | [[Category: DMU]] | ||
[[Category: composite active site]] | [[Category: composite active site]] | ||
[[Category: cysteine protease]] | [[Category: cysteine protease]] | ||
[[Category: dimer]] | [[Category: dimer]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:28:37 2008'' |
Revision as of 00:28, 31 March 2008
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| , resolution 2.28Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Structure of the catalytic domain of hepatitis C virus NS2
Overview
Hepatitis C virus is a major global health problem affecting an estimated 170 million people worldwide. Chronic infection is common and can lead to cirrhosis and liver cancer. There is no vaccine available and current therapies have met with limited success. The viral RNA genome encodes a polyprotein that includes two proteases essential for virus replication. The NS2-3 protease mediates a single cleavage at the NS2/NS3 junction, whereas the NS3-4A protease cleaves at four downstream sites in the polyprotein. NS3-4A is characterized as a serine protease with a chymotrypsin-like fold, but the enzymatic mechanism of the NS2-3 protease remains unresolved. Here we report the crystal structure of the catalytic domain of the NS2-3 protease at 2.3 A resolution. The structure reveals a dimeric cysteine protease with two composite active sites. For each active site, the catalytic histidine and glutamate residues are contributed by one monomer, and the nucleophilic cysteine by the other. The carboxy-terminal residues remain coordinated in the two active sites, predicting an inactive post-cleavage form. Proteolysis through formation of a composite active site occurs in the context of the viral polyprotein expressed in mammalian cells. These features offer unexpected insights into polyprotein processing by hepatitis C virus and new opportunities for antiviral drug design.
About this Structure
2HD0 is a Single protein structure of sequence from Hepatitis c virus. Full crystallographic information is available from OCA.
Reference
Structure of the catalytic domain of the hepatitis C virus NS2-3 protease., Lorenz IC, Marcotrigiano J, Dentzer TG, Rice CM, Nature. 2006 Aug 17;442(7104):831-5. Epub 2006 Jul 23. PMID:16862121
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