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1sh0

From Proteopedia

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{{STRUCTURE_1sh0| PDB=1sh0 | SCENE= }}
{{STRUCTURE_1sh0| PDB=1sh0 | SCENE= }}
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'''Crystal Structure of Norwalk Virus Polymerase (Triclinic)'''
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===Crystal Structure of Norwalk Virus Polymerase (Triclinic)===
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==Overview==
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Norwalk virus is a major cause of acute gastroenteritis for which effective treatments are sorely lacking. To provide a basis for the rational design of novel antiviral agents, the main replication enzyme in Norwalk virus, the virally encoded RNA-dependent RNA polymerase (RdRP), has been expressed in an enzymatically active form, and its structure has been crystallographically determined both in the presence and absence of divalent metal cations. Although the overall fold of the enzyme is similar to that seen previously in the RdRP from rabbit hemorrhagic disease virus, the carboxyl terminus, surprisingly, is located in the active site cleft in five independent copies of the protein in three distinct crystal forms. The location of this carboxyl-terminal segment appears to interfere with the binding of double-stranded RNA in the active site cleft and may play a role in the initiation of RNA synthesis or mediate interactions with accessory replication proteins.
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(as it appears on PubMed at http://www.pubmed.gov), where 14764591 is the PubMed ID number.
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{{ABSTRACT_PUBMED_14764591}}
==About this Structure==
==About this Structure==
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[[Category: Rna polymerase]]
[[Category: Rna polymerase]]
[[Category: Viral replication enzyme]]
[[Category: Viral replication enzyme]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:41:45 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 17:03:58 2008''

Revision as of 14:03, 28 July 2008

Image:1sh0.png

Template:STRUCTURE 1sh0

Crystal Structure of Norwalk Virus Polymerase (Triclinic)

Template:ABSTRACT PUBMED 14764591

About this Structure

1SH0 is a Single protein structure of sequence from Norwalk virus. Full crystallographic information is available from OCA.

Reference

Crystal structure of norwalk virus polymerase reveals the carboxyl terminus in the active site cleft., Ng KK, Pendas-Franco N, Rojo J, Boga JA, Machin A, Alonso JM, Parra F, J Biol Chem. 2004 Apr 16;279(16):16638-45. Epub 2004 Feb 5. PMID:14764591

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