1jxp
From Proteopedia
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[[Image:1jxp.jpg|left|200px]] | [[Image:1jxp.jpg|left|200px]] | ||
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'''BK STRAIN HEPATITIS C VIRUS (HCV) NS3-NS4A''' | '''BK STRAIN HEPATITIS C VIRUS (HCV) NS3-NS4A''' | ||
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==Reference== | ==Reference== | ||
Complex of NS3 protease and NS4A peptide of BK strain hepatitis C virus: a 2.2 A resolution structure in a hexagonal crystal form., Yan Y, Li Y, Munshi S, Sardana V, Cole JL, Sardana M, Steinkuehler C, Tomei L, De Francesco R, Kuo LC, Chen Z, Protein Sci. 1998 Apr;7(4):837-47. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9568891 9568891] | Complex of NS3 protease and NS4A peptide of BK strain hepatitis C virus: a 2.2 A resolution structure in a hexagonal crystal form., Yan Y, Li Y, Munshi S, Sardana V, Cole JL, Sardana M, Steinkuehler C, Tomei L, De Francesco R, Kuo LC, Chen Z, Protein Sci. 1998 Apr;7(4):837-47. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9568891 9568891] | ||
- | [[Category: Hepatitis c virus genotype 1b (isolate bk)]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Chen, Z.]] | [[Category: Chen, Z.]] | ||
[[Category: Munshi, S.]] | [[Category: Munshi, S.]] | ||
[[Category: Yan, Y.]] | [[Category: Yan, Y.]] | ||
- | [[Category: | + | [[Category: Hydrolase]] |
- | [[Category: | + | [[Category: Serine proteinase]] |
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Revision as of 19:03, 2 May 2008
BK STRAIN HEPATITIS C VIRUS (HCV) NS3-NS4A
Overview
The crystal structure of the NS3 protease of the hepatitis C virus (BK strain) has been determined in the space group P6(3)22 to a resolution of 2.2 A. This protease is bound with a 14-mer peptide representing the central region of the NS4A protein. There are two molecules of the NS3(1-180)-NS4A(21'-34') complex per asymmetric unit. Each displays a familiar chymotrypsin-like fold that includes two beta-barrel domains and four short alpha-helices. The catalytic triad (Ser-139, His-57, and Asp-81) is located in the crevice between the beta-barrel domains. The NS4A peptide forms an almost completely enclosed peptide surface association with the protease. In contrast to the reported H strain complex of NS3 protease-NS4A peptide in a trigonal crystal form (Kim JL et al., 1996, Cell 87:343-355), the N-terminus of the NS3 protease is well-ordered in both molecules in the asymmetric unit of our hexagonal crystal form. The folding of the N-terminal region of the NS3 protease is due to the formation of a three-helix bundle as a result of crystal packing. When compared with the unbound structure (Love RA et al., 1996, Cell 87:331-342), the binding of the NS4A peptide leads to the ordering of the N-terminal 28 residues of the NS3 protease into a beta-strand and an alpha-helix and also causes local rearrangements important for a catalytically favorable conformation at the active site. Our analysis provides experimental support for the proposal that binding of an NS4A-mimicking peptide, which increases catalytic rates, is necessary but not sufficient for formation of a well-ordered, compact and, hence, highly active protease molecule.
About this Structure
1JXP is a Protein complex structure of sequences from Hepatitis c virus genotype 1b (isolate bk). Full crystallographic information is available from OCA.
Reference
Complex of NS3 protease and NS4A peptide of BK strain hepatitis C virus: a 2.2 A resolution structure in a hexagonal crystal form., Yan Y, Li Y, Munshi S, Sardana V, Cole JL, Sardana M, Steinkuehler C, Tomei L, De Francesco R, Kuo LC, Chen Z, Protein Sci. 1998 Apr;7(4):837-47. PMID:9568891 Page seeded by OCA on Fri May 2 22:03:10 2008