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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 ==
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| 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>
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| <div class="pdbe-citations 1xok" style="background-color:#fffaf0;"></div>
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| == References ==
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| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
