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Crystal structure of zinc‐finger domain of Nanos and its functional implications

Crystal structure of zinc‐finger domain of Nanos and its functional implications 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. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png EMBO Reports Wiley

Crystal structure of zinc‐finger domain of Nanos and its functional implications

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References (46)

Publisher
Wiley
Copyright
Copyright © 2013 Wiley Periodicals, Inc
ISSN
1469-221X
eISSN
1469-3178
DOI
10.1038/embor.2010.155
pmid
20948543
Publisher site
See Article on Publisher Site

Abstract

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.

Journal

EMBO ReportsWiley

Published: Nov 1, 2010

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