This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1jxp

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1jxp.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1jxp.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1jxp| PDB=1jxp | SCENE= }}
{{STRUCTURE_1jxp| PDB=1jxp | SCENE= }}
-
'''BK STRAIN HEPATITIS C VIRUS (HCV) NS3-NS4A'''
+
===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.
+
The line below this paragraph, {{ABSTRACT_PUBMED_9568891}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 9568891 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_9568891}}
==About this Structure==
==About this Structure==
Line 26: Line 30:
[[Category: Hydrolase]]
[[Category: Hydrolase]]
[[Category: Serine proteinase]]
[[Category: Serine proteinase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 22:03:10 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 19:47:27 2008''

Revision as of 16:47, 28 July 2008

Image:1jxp.png

Template:STRUCTURE 1jxp

BK STRAIN HEPATITIS C VIRUS (HCV) NS3-NS4A

Template:ABSTRACT PUBMED 9568891

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 Mon Jul 28 19:47:27 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1jxp"
Personal tools