3alr: Difference between revisions

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== Function ==
== Function ==
[https://www.uniprot.org/uniprot/Q4QRE8_DANRE Q4QRE8_DANRE]  
[https://www.uniprot.org/uniprot/Q4QRE8_DANRE Q4QRE8_DANRE]  
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== Publication Abstract from PubMed ==
Nanos is an RNA-binding protein that is involved in the development and maintenance of germ cells. In combination with Pumilio, Nanos binds to the 3' untranslated region of a messenger RNA and represses its translation. Nanos has two conserved Cys-Cys-His-Cys zinc-finger motifs that are indispensable for its function. In this study, we have determined the crystal structure of the zinc-finger domain of zebrafish Nanos, for the first time revealing that Nanos adopts a novel zinc-finger structure. In addition, Nanos has a conserved basic surface that is directly involved in RNA binding. Our results provide the structural basis for further studies to clarify Nanos function.
Crystal structure of zinc-finger domain of Nanos and its functional implications.,Hashimoto H, Hara K, Hishiki A, Kawaguchi S, Shichijo N, Nakamura K, Unzai S, Tamaru Y, Shimizu T, Sato M EMBO Rep. 2010 Nov;11(11):848-53. Epub 2010 Oct 15. PMID:20948543<ref>PMID:20948543</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 14:01, 13 March 2024

Crystal structure of Nanos

3alr, resolution 2.10Å

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