1a1r: Difference between revisions

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==Overview==
==Overview==
An estimated 1% of the global human population is infected by hepatitis C, viruses (HCVs), and there are no broadly effective treatments for the, debilitating progression of chronic hepatitis C. A serine protease located, within the HCV NS3 protein processes the viral polyprotein at four, specific sites and is considered essential for replication. Thus, it, emerges as an attractive target for drug design. We report here the 2.5, angstrom resolution X-ray crystal structure of the NS3 protease domain, complexed with a synthetic NS4A activator peptide. The protease has a, chymotrypsin-like fold and features a tetrahedrally coordinated metal ion, distal to the active site. The NS4A peptide intercalates within a beta, sheet of the enzyme core.
An estimated 1% of the global human population is infected by hepatitis C viruses (HCVs), and there are no broadly effective treatments for the debilitating progression of chronic hepatitis C. A serine protease located within the HCV NS3 protein processes the viral polyprotein at four specific sites and is considered essential for replication. Thus, it emerges as an attractive target for drug design. We report here the 2.5 angstrom resolution X-ray crystal structure of the NS3 protease domain complexed with a synthetic NS4A activator peptide. The protease has a chymotrypsin-like fold and features a tetrahedrally coordinated metal ion distal to the active site. The NS4A peptide intercalates within a beta sheet of the enzyme core.


==About this Structure==
==About this Structure==
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[[Category: Gb virus c]]
[[Category: Gb virus c]]
[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Caron, P.R.]]
[[Category: Caron, P R.]]
[[Category: Chambers, S.P.]]
[[Category: Chambers, S P.]]
[[Category: Dwyer, M.D.]]
[[Category: Dwyer, M D.]]
[[Category: Fox, T.]]
[[Category: Fox, T.]]
[[Category: Harbeson, S.L.]]
[[Category: Harbeson, S L.]]
[[Category: Kim, J.L.]]
[[Category: Kim, J L.]]
[[Category: Landro, J.A.]]
[[Category: Landro, J A.]]
[[Category: Lepre, C.A.]]
[[Category: Lepre, C A.]]
[[Category: Lin, C.]]
[[Category: Lin, C.]]
[[Category: Malley, E.T.O.]]
[[Category: Malley, E T.O.]]
[[Category: Markland, W.]]
[[Category: Markland, W.]]
[[Category: Morgenstern, K.A.]]
[[Category: Morgenstern, K A.]]
[[Category: Murcko, M.A.]]
[[Category: Murcko, M A.]]
[[Category: Rice, C.M.]]
[[Category: Rice, C M.]]
[[Category: Thomson, J.A.]]
[[Category: Thomson, J A.]]
[[Category: ZN]]
[[Category: ZN]]
[[Category: cofactor peptide]]
[[Category: cofactor peptide]]
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[[Category: viral protein]]
[[Category: viral protein]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:28:38 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:39:51 2008''

Revision as of 12:39, 21 February 2008

File:1a1r.gif


1a1r, resolution 2.5Å

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HCV NS3 PROTEASE DOMAIN:NS4A PEPTIDE COMPLEX

OverviewOverview

An estimated 1% of the global human population is infected by hepatitis C viruses (HCVs), and there are no broadly effective treatments for the debilitating progression of chronic hepatitis C. A serine protease located within the HCV NS3 protein processes the viral polyprotein at four specific sites and is considered essential for replication. Thus, it emerges as an attractive target for drug design. We report here the 2.5 angstrom resolution X-ray crystal structure of the NS3 protease domain complexed with a synthetic NS4A activator peptide. The protease has a chymotrypsin-like fold and features a tetrahedrally coordinated metal ion distal to the active site. The NS4A peptide intercalates within a beta sheet of the enzyme core.

About this StructureAbout this Structure

1A1R is a Protein complex structure of sequences from Gb virus c with as ligand. Known structural/functional Sites: , , and . Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of the hepatitis C virus NS3 protease domain complexed with a synthetic NS4A cofactor peptide., Kim JL, Morgenstern KA, Lin C, Fox T, Dwyer MD, Landro JA, Chambers SP, Markland W, Lepre CA, O'Malley ET, Harbeson SL, Rice CM, Murcko MA, Caron PR, Thomson JA, Cell. 1996 Oct 18;87(2):343-55. PMID:8861917

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