1bt7

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[[Image:1bt7.gif|left|200px]]<br /><applet load="1bt7" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1bt7.gif|left|200px]]
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caption="1bt7" />
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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'''<br />
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{{Structure
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|PDB= 1bt7 |SIZE=350|CAPTION= <scene name='initialview01'>1bt7</scene>
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|SITE= <scene name='pdbsite=CTS:Catalytic+Site'>CTS</scene> and <scene name='pdbsite=ZNB:Zn+Binding+Site'>ZNB</scene>
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|LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene>
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|ACTIVITY=
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|GENE=
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}}
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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'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1BT7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gb_virus_c Gb virus c] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Sites: <scene name='pdbsite=CTS:Catalytic+Site'>CTS</scene> and <scene name='pdbsite=ZNB:Zn+Binding+Site'>ZNB</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BT7 OCA].
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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==
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=10366511 10366511]
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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]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:58:49 2008''
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''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


PDB ID 1bt7

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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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