1xok
From Proteopedia
(Difference between revisions)
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== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/CAPSD_AMVYS CAPSD_AMVYS] Capsid protein. Binds to the to the 3' end of the nonpolyadenylated viral RNA and is involved in viral RNA translation initiation. Probably binds RNA and plays a role in packaging (By similarity). | [https://www.uniprot.org/uniprot/CAPSD_AMVYS CAPSD_AMVYS] Capsid protein. Binds to the to the 3' end of the nonpolyadenylated viral RNA and is involved in viral RNA translation initiation. Probably binds RNA and plays a role in packaging (By similarity). | ||
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| - | == Publication Abstract from PubMed == | ||
| - | Alfalfa mosaic virus genomic RNAs are infectious only when the viral coat protein binds to the RNA 3' termini. The crystal structure of an alfalfa mosaic virus RNA-peptide complex reveals that conserved AUGC repeats and Pro-Thr-x-Arg-Ser-x-x-Tyr coat protein amino acids cofold upon interacting. Alternating AUGC residues have opposite orientation, and they base pair in different adjacent duplexes. Localized RNA backbone reversals stabilized by arginine-guanine interactions place the adenosines and guanines in reverse order in the duplex. The results suggest that a uniform, organized 3' conformation, similar to that found on viral RNAs with transfer RNA-like ends, may be essential for replication. | ||
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| - | Cofolding organizes alfalfa mosaic virus RNA and coat protein for replication.,Guogas LM, Filman DJ, Hogle JM, Gehrke L Science. 2004 Dec 17;306(5704):2108-11. PMID:15604410<ref>PMID:15604410</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
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| - | <div class="pdbe-citations 1xok" style="background-color:#fffaf0;"></div> | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
crystal structure of alfalfa mosaic virus RNA 3'UTR in complex with coat protein N terminal peptide
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