Publication Date:
1989-07-14
Description:
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.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chen, Z G -- Stauffacher, C -- Li, Y -- Schmidt, T -- Bomu, W -- Kamer, G -- Shanks, M -- Lomonossoff, G -- Johnson, J E -- AI18764/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1989 Jul 14;245(4914):154-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Sciences, Purdue University, West Lafayette, Indiana 47907.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2749253" target="_blank"〉PubMed〈/a〉
Keywords:
Amino Acid Sequence
;
Capsid/*metabolism/ultrastructure
;
Crystallography
;
Electron Probe Microanalysis
;
Electrophoresis, Polyacrylamide Gel
;
Macromolecular Substances
;
Molecular Sequence Data
;
Mosaic Viruses/*analysis/genetics/ultrastructure
;
Plant Viruses/*analysis/genetics/ultrastructure
;
Protein Conformation
;
RNA, Viral/*metabolism/ultrastructure
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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