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1bt7
From Proteopedia
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| - | [[Image:1bt7.gif|left|200px]]< | + | [[Image:1bt7.gif|left|200px]] |
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| - | '''THE SOLUTION NMR STRUCTURE OF THE N-TERMINAL PROTEASE DOMAIN OF THE HEPATITIS C VIRUS (HCV) NS3-PROTEIN, FROM BK STRAIN, 20 STRUCTURES''' | + | {{Structure |
| + | |PDB= 1bt7 |SIZE=350|CAPTION= <scene name='initialview01'>1bt7</scene> | ||
| + | |SITE= <scene name='pdbsite=CTS:Catalytic+Site'>CTS</scene> and <scene name='pdbsite=ZNB:Zn+Binding+Site'>ZNB</scene> | ||
| + | |LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''THE SOLUTION NMR STRUCTURE OF THE N-TERMINAL PROTEASE DOMAIN OF THE HEPATITIS C VIRUS (HCV) NS3-PROTEIN, FROM BK STRAIN, 20 STRUCTURES''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1BT7 is a [ | + | 1BT7 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Gb_virus_c Gb virus c]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BT7 OCA]. |
==Reference== | ==Reference== | ||
| - | The solution structure of the N-terminal proteinase domain of the hepatitis C virus (HCV) NS3 protein provides new insights into its activation and catalytic mechanism., Barbato G, Cicero DO, Nardi MC, Steinkuhler C, Cortese R, De Francesco R, Bazzo R, J Mol Biol. 1999 Jun 4;289(2):371-84. PMID:[http:// | + | The solution structure of the N-terminal proteinase domain of the hepatitis C virus (HCV) NS3 protein provides new insights into its activation and catalytic mechanism., Barbato G, Cicero DO, Nardi MC, Steinkuhler C, Cortese R, De Francesco R, Bazzo R, J Mol Biol. 1999 Jun 4;289(2):371-84. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10366511 10366511] |
[[Category: Gb virus c]] | [[Category: Gb virus c]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: viral non-structural protein]] | [[Category: viral non-structural protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:15:31 2008'' |
Revision as of 08:15, 20 March 2008
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THE SOLUTION NMR STRUCTURE OF THE N-TERMINAL PROTEASE DOMAIN OF THE HEPATITIS C VIRUS (HCV) NS3-PROTEIN, FROM BK STRAIN, 20 STRUCTURES
Overview
The solution structure of the hepatitis C virus (BK strain) NS3 protein N-terminal domain (186 residues) has been solved by NMR spectroscopy. The protein is a serine protease with a chymotrypsin-type fold, and is involved in the maturation of the viral polyprotein. Despite the knowledge that its activity is enhanced by the action of a viral protein cofactor, NS4A, the mechanism of activation is not yet clear. The analysis of the folding in solution and the differences from the crystallographic structures allow the formulation of a model in which, in addition to the NS4A cofactor, the substrate plays an important role in the activation of the catalytic mechanism. A unique structural feature is the presence of a zinc-binding site exposed on the surface, subject to a slow conformational exchange process.
About this Structure
1BT7 is a Single protein structure of sequence from Gb virus c. Full crystallographic information is available from OCA.
Reference
The solution structure of the N-terminal proteinase domain of the hepatitis C virus (HCV) NS3 protein provides new insights into its activation and catalytic mechanism., Barbato G, Cicero DO, Nardi MC, Steinkuhler C, Cortese R, De Francesco R, Bazzo R, J Mol Biol. 1999 Jun 4;289(2):371-84. PMID:10366511
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