1a1q

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[[Image:1a1q.gif|left|200px]]
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{{STRUCTURE_1a1q| PDB=1a1q | SCENE= }}
{{STRUCTURE_1a1q| PDB=1a1q | SCENE= }}
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'''HEPATITIS C VIRUS NS3 PROTEINASE'''
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===HEPATITIS C VIRUS NS3 PROTEINASE===
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==Overview==
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During replication of hepatitis C virus (HCV), the final steps of polyprotein processing are performed by a viral proteinase located in the N-terminal one-third of nonstructural protein 3. The structure of NS3 proteinase from HCV BK strain was determined by X-ray crystallography at 2.4 angstrom resolution. NS3P folds as a trypsin-like proteinase with two beta barrels and a catalytic triad of His-57, Asp-81, Ser-139. The structure has a substrate-binding site consistent with the cleavage specificity of the enzyme. Novel features include a structural zinc-binding site and a long N-terminus that interacts with neighboring molecules by binding to a hydrophobic surface patch.
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(as it appears on PubMed at http://www.pubmed.gov), where 8861916 is the PubMed ID number.
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{{ABSTRACT_PUBMED_8861916}}
==About this Structure==
==About this Structure==
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[[Category: Hydrolase]]
[[Category: Hydrolase]]
[[Category: Serine protease]]
[[Category: Serine protease]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 09:40:30 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 15:48:20 2008''

Revision as of 12:48, 30 June 2008

Template:STRUCTURE 1a1q

HEPATITIS C VIRUS NS3 PROTEINASE

Template:ABSTRACT PUBMED 8861916

About this Structure

1A1Q is a Single protein structure of sequence from Hepatitis c virus. Full crystallographic information is available from OCA.

Reference

The crystal structure of hepatitis C virus NS3 proteinase reveals a trypsin-like fold and a structural zinc binding site., Love RA, Parge HE, Wickersham JA, Hostomsky Z, Habuka N, Moomaw EW, Adachi T, Hostomska Z, Cell. 1996 Oct 18;87(2):331-42. PMID:8861916

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