1uty: Difference between revisions

Revision as of 12:39, 28 July 2008

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Template:STRUCTURE 1uty

CRYSTAL STRUCTURE OF THE RNA BINDING DOMAIN OF BLUETONGUE VIRUS NON-STRUCTURAL PROTEIN 2(NS2)CRYSTAL STRUCTURE OF THE RNA BINDING DOMAIN OF BLUETONGUE VIRUS NON-STRUCTURAL PROTEIN 2(NS2)

Template:ABSTRACT PUBMED 15155766

About this StructureAbout this Structure

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

ReferenceReference

Structure and assembly of the RNA binding domain of bluetongue virus non-structural protein 2., Butan C, Van Der Zandt H, Tucker PA, J Biol Chem. 2004 Sep 3;279(36):37613-21. Epub 2004 May 20. PMID:15155766

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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 {{STRUCTURE_1uty|  PDB=1uty  |  SCENE=  }}
-'''CRYSTAL STRUCTURE OF THE RNA BINDING DOMAIN OF BLUETONGUE VIRUS NON-STRUCTURAL PROTEIN 2(NS2)'''
+===CRYSTAL STRUCTURE OF THE RNA BINDING DOMAIN OF BLUETONGUE VIRUS NON-STRUCTURAL PROTEIN 2(NS2)===
-==Overview==
+<!--
-Bluetongue virus non-structural protein 2 belongs to a class of highly conserved proteins found in orbiviruses of the Reoviridae family. Non-structural protein 2 forms large multimeric complexes and localizes to cytoplasmic inclusions in infected cells. It is able to bind single-stranded RNA non-specifically, and it has been suggested that the protein is involved in the selection and condensation of the Bluetongue virus RNA segments prior to genome encapsidation. We have determined the x-ray structure of the N-terminal domain (sufficient for the RNA binding ability of non-structural protein 2) to 2.4 A resolution using anomalous scattering methods. Crystals of this apparently insoluble domain were obtained by in situ proteolysis of a soluble construct. The asymmetric unit shows two monomers related by non-crystallographic symmetry, with each monomer folded as a beta sandwich with a unique topology. The crystal structure reveals extensive monomer-monomer interactions, which explain the ability of the protein to self-assemble into large homomultimeric complexes. Of the entire surface area of the monomer, one-third is used to create the interfaces of the curved multimeric assembly observed in the x-ray structure. The structure reported here shows how the N-terminal domain would be able to bind single-stranded RNA non-specifically protecting the bound regions in a heterogeneous multimeric but not polymeric complex.
+The line below this paragraph, {{ABSTRACT_PUBMED_15155766}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15155766 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_15155766}}
 ==About this Structure==
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 [[Category: Rna binding protein]]
 [[Category: Viral protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 11:41:08 2008''
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