1xok: 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.
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>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
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</StructureSection>
</StructureSection>

Latest revision as of 08:52, 14 February 2024

crystal structure of alfalfa mosaic virus RNA 3'UTR in complex with coat protein N terminal peptide

1xok, resolution 3.00Å

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