1ng0: Difference between revisions

Revision as of 08:39, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1ng0.png

Template:STRUCTURE 1ng0

The three-dimensional structure of Cocksfoot mottle virus at 2.7A resolutionThe three-dimensional structure of Cocksfoot mottle virus at 2.7A resolution

Template:ABSTRACT PUBMED 12781716

About this StructureAbout this Structure

1NG0 is a Single protein structure of sequence from Cocksfoot mottle virus. Full crystallographic information is available from OCA.

ReferenceReference

The three-dimensional structure of cocksfoot mottle virus at 2.7 A resolution., Tars K, Zeltins A, Liljas L, Virology. 2003 Jun 5;310(2):287-97. PMID:12781716

Page seeded by OCA on Tue Jul 29 08:39:23 2008

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

OCA

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-'''The three-dimensional structure of Cocksfoot mottle virus at 2.7A resolution'''
+===The three-dimensional structure of Cocksfoot mottle virus at 2.7A resolution===
-==Overview==
+<!--
-Cocksfoot mottle virus is a plant virus that belongs to the genus Sobemovirus. The structure of the virus has been determined at 2.7 A resolution. The icosahedral capsid has T = 3 quasisymmetry and 180 copies of the coat protein. Except for a couple of stacked bases, the viral RNA is not visible in the electron density map. The coat protein has a jelly-roll beta-sandwich fold and its conformation is very similar to that of other sobemoviruses and tobacco necrosis virus. The N-terminal arm of one of the three quasiequivalent subunits is partly ordered and follows the same path in the capsid as the arm in rice yellow mottle virus, another sobemovirus. In other sobemoviruses, the ordered arm follows a different path, but in both cases the arms from three subunits meet and form a similar structure at a threefold axis. A comparison of the structures and sequences of viruses in this family shows that the only conserved parts of the protein-protein interfaces are those that form binding sites for calcium ions. Still, the relative orientations and position of the subunits are maintained.
+The line below this paragraph, {{ABSTRACT_PUBMED_12781716}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_12781716}}
 ==About this Structure==
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 [[Category: Sobemovirus]]
 [[Category: Virus assembly]]
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