PROSITE documentation PDOC51522Zinc finger nanos-type profile
Nanos is a highly conserved RNA-binding protein in higher eukaryotes and functions as a key regulatory protein in translational control using a 3' untranslated region during the development and maintenance of germ cells. Nanos comprises a non-conserved amino-terminus and highly conserved carboxy-terminal regions. The C-terminal region has two conserved Cys-Cys-His-Cys (CCHC)-type zinc-finger motifs that are indispensable for nanos function [1,2,3].
The structure of the nanos-type zinc finger is composed of two independent zinc-finger (ZF) lobes, the N-terminal ZF1 and the C-terminal ZF2, which are connected by a linker helix (see <PDB:3ALR>) [3]. These lobes create a large cleft. Zinc ions in ZF1 and ZF2 are bound to the CCHC motif by tetrahedral coordination.
The profile we developed covers the entire nanos-type zinc finger.
Last update:February 2011 / First entry.
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PROSITE method (with tools and information) covered by this documentation:
1 | Authors | Mosquera L. Forristall C. Zhou Y. King M.L. |
Title | A mRNA localized to the vegetal cortex of Xenopus oocytes encodes a protein with a nanos-like zinc finger domain. | |
Source | Development 117:377-386(1993). | |
PubMed ID | 8223259 |
2 | Authors | Subramaniam K. Seydoux G. |
Title | nos-1 and nos-2, two genes related to Drosophila nanos, regulate primordial germ cell development and survival in Caenorhabditis elegans. | |
Source | Development 126:4861-4871(1999). | |
PubMed ID | 10518502 |
3 | Authors | Hashimoto H. Hara K. Hishiki A. Kawaguchi S. Shichijo N. Nakamura K. Unzai S. Tamaru Y. Shimizu T. Sato M. |
Title | Crystal structure of zinc-finger domain of Nanos and its functional implications. | |
Source | EMBO. Rep. 11:848-853(2010). | |
PubMed ID | 20948543 | |
DOI | 10.1038/embor.2010.155 |
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