Protein-RNA interactions in an icosahedral virus at 3.0 Angstrom resolution
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 stereo-chemical properties. Interact...
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| Veröffentlicht in: | Science (American Association for the Advancement of Science) 1989-07, Vol.245 (4914), p.154-159 |
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| container_title | Science (American Association for the Advancement of Science) |
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| creator | Chen, Zhongguo Stauffacher, Cynthia Li, Yunge Schmidt, Tim Bomu, Wu Kamer, Greg Shanks, Michael Lomonossoff, George Johnson, John E |
| 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 stereo-chemical 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. |
| format | Article |
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The RNA displaying icosahedral symmetry is single-stranded with well-defined polarity and stereo-chemical 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.</description><identifier>ISSN: 0036-8075</identifier><identifier>EISSN: 1095-9203</identifier><language>eng</language><publisher>American Association for the Advancement of Science</publisher><subject>Picornaviruses ; Protein binding ; RNA</subject><ispartof>Science (American Association for the Advancement of Science), 1989-07, Vol.245 (4914), p.154-159</ispartof><rights>COPYRIGHT 1989 American Association for the Advancement of Science</rights><rights>COPYRIGHT 1989 American Association for the Advancement of Science</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,778,782</link.rule.ids></links><search><creatorcontrib>Chen, Zhongguo</creatorcontrib><creatorcontrib>Stauffacher, Cynthia</creatorcontrib><creatorcontrib>Li, Yunge</creatorcontrib><creatorcontrib>Schmidt, Tim</creatorcontrib><creatorcontrib>Bomu, Wu</creatorcontrib><creatorcontrib>Kamer, Greg</creatorcontrib><creatorcontrib>Shanks, Michael</creatorcontrib><creatorcontrib>Lomonossoff, George</creatorcontrib><creatorcontrib>Johnson, John E</creatorcontrib><title>Protein-RNA interactions in an icosahedral virus at 3.0 Angstrom resolution</title><title>Science (American Association for the Advancement of Science)</title><addtitle>Science</addtitle><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. 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| fulltext | fulltext |
| identifier | ISSN: 0036-8075 |
| ispartof | Science (American Association for the Advancement of Science), 1989-07, Vol.245 (4914), p.154-159 |
| issn | 0036-8075 1095-9203 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_15303548 |
| source | American Association for the Advancement of Science; Jstor Complete Legacy |
| subjects | Picornaviruses Protein binding RNA |
| title | Protein-RNA interactions in an icosahedral virus at 3.0 Angstrom resolution |
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