1bmv
From Proteopedia
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'''PROTEIN-RNA INTERACTIONS IN AN ICOSAHEDRAL VIRUS AT 3.0 ANGSTROMS RESOLUTION''' | '''PROTEIN-RNA INTERACTIONS IN AN ICOSAHEDRAL VIRUS AT 3.0 ANGSTROMS RESOLUTION''' | ||
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[[Category: Shanks, M.]] | [[Category: Shanks, M.]] | ||
[[Category: Stauffacher, C.]] | [[Category: Stauffacher, C.]] | ||
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| - | [[Category: | + | [[Category: Protein-rna complex]] |
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Revision as of 08:42, 2 May 2008
PROTEIN-RNA INTERACTIONS IN AN ICOSAHEDRAL VIRUS AT 3.0 ANGSTROMS RESOLUTION
Overview
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 Structure
1BMV is a Protein complex structure of sequences from Bean pod mottle virus. Full crystallographic information is available from OCA.
Reference
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 Page seeded by OCA on Fri May 2 11:42:42 2008
