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.

Purification, crystallization and initial X-ray diffraction study of the zinc-finger domain of zebrafish Nanos.

Nanos is a highly conserved RNA-binding protein in higher eukaryotes and acts as a key regulator protein involved in translational control utilizing the 3' untranslated region of mRNA. The C-terminal domain of Nanos has two conserved and novel CCHC-type zinc-finger motifs that are responsible for the function of Nanos. To clarify the structural basis of the function of Nanos, the C-terminal domain (residues 59-159) of zebrafish Nanos was overexpressed, purified and crystallized.