1un6
From Proteopedia
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THE CRYSTAL STRUCTURE OF A ZINC FINGER- RNA COMPLEX REVEALS TWO MODES OF MOLECULAR RECOGNITION
Overview
Zinc-finger proteins of the classical Cys2His2 type are the most, frequently used class of transcription factor and account for about 3% of, genes in the human genome. The zinc-finger motif was discovered during, biochemical studies on the transcription factor TFIIIA, which regulates, the 5S ribosomal RNA genes of Xenopus laevis. Zinc-fingers mostly interact, with DNA, but TFIIIA binds not only specifically to the promoter DNA, but, also to 5S RNA itself. Increasing evidence indicates that zinc-fingers are, more widely used to recognize RNA. There have been numerous structural, studies on DNA binding, but none on RNA binding by zinc-finger proteins., Here we report the crystal structure of a three-finger complex with 61, bases of RNA, derived from the central regions of the complete nine-finger, TFIIIA-5S RNA complex. The structure reveals two modes of zinc-finger, binding, both of which differ from that in common use for DNA: first, the, zinc-fingers interact with the backbone of a double helix; and second, the, zinc-fingers specifically recognize individual bases positioned for access, in otherwise intricately folded 'loop' regions of the RNA.
About this Structure
1UN6 is a Single protein structure of sequence from Xenopus laevis with and as ligands. The following page contains interesting information on the relation of 1UN6 with [Zinc Fingers]. Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
Crystal structure of a zinc-finger-RNA complex reveals two modes of molecular recognition., Lu D, Searles MA, Klug A, Nature. 2003 Nov 6;426(6962):96-100. PMID:14603324
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