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1a1q
From Proteopedia
(New page: 200px<br /><applet load="1a1q" size="450" color="white" frame="true" align="right" spinBox="true" caption="1a1q, resolution 2.4Å" /> '''HEPATITIS C VIRUS NS3...) |
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| - | [[Image:1a1q.gif|left|200px]]<br /><applet load="1a1q" size=" | + | [[Image:1a1q.gif|left|200px]]<br /><applet load="1a1q" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1a1q, resolution 2.4Å" /> | caption="1a1q, resolution 2.4Å" /> | ||
'''HEPATITIS C VIRUS NS3 PROTEINASE'''<br /> | '''HEPATITIS C VIRUS NS3 PROTEINASE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | During replication of hepatitis C virus (HCV), the final steps of | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1A1Q is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Hepatitis_c_virus Hepatitis c virus] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1A1Q is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Hepatitis_c_virus Hepatitis c virus] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A1Q OCA]. |
==Reference== | ==Reference== | ||
| Line 17: | Line 17: | ||
[[Category: Hostomska, Z.]] | [[Category: Hostomska, Z.]] | ||
[[Category: Hostomsky, Z.]] | [[Category: Hostomsky, Z.]] | ||
| - | [[Category: Love, R | + | [[Category: Love, R A.]] |
| - | [[Category: Moomaw, E | + | [[Category: Moomaw, E W.]] |
| - | [[Category: Parge, H | + | [[Category: Parge, H E.]] |
| - | [[Category: Wickersham, J | + | [[Category: Wickersham, J A.]] |
[[Category: ZN]] | [[Category: ZN]] | ||
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
[[Category: serine protease]] | [[Category: serine protease]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:39:52 2008'' |
Revision as of 09:39, 21 February 2008
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HEPATITIS C VIRUS NS3 PROTEINASE
Overview
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.
About this Structure
1A1Q is a Single protein structure of sequence from Hepatitis c virus with as ligand. 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
Page seeded by OCA on Thu Feb 21 11:39:52 2008
