1bmv

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Revision as of 12:38, 20 November 2007 by OCA (talk | contribs) (New page: left|200px<br /><applet load="1bmv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bmv, resolution 3.000Å" /> '''PROTEIN-RNA INTERAC...)
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File:1bmv.gif


1bmv, resolution 3.000Å

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PROTEIN-RNA INTERACTIONS IN AN ICOSAHEDRAL VIRUS AT 3.0 ANGSTROMS RESOLUTION

OverviewOverview

Nearly 20 percent of the packaged RNA in bean-pod mottle virus (BPMV), binds to the capsid interior in a symmetric fashion and is clearly visible, in the electron density map. The RNA displaying icosahedral symmetry is, single-stranded with well-defined polarity and stereochemical properties., Interactions with protein are dominated by nonbonding forces with few, specific contacts. The tertiary and quaternary structures of the BPMV, capsid proteins are similar to those observed in animal picornaviruses, supporting the close relation between plant comoviruses and animal, picornaviruses established by previous biological studies.

About this StructureAbout this Structure

1BMV is a Protein complex structure of sequences from Bean pod mottle virus. Full crystallographic information is available from OCA.

ReferenceReference

Protein-RNA interactions in an icosahedral virus at 3.0 A resolution., Chen ZG, Stauffacher C, Li Y, Schmidt T, Bomu W, Kamer G, Shanks M, Lomonossoff G, Johnson JE, Science. 1989 Jul 14;245(4914):154-9. PMID:2749253

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