1un6
From Proteopedia
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==Overview== | ==Overview== | ||
| - | Zinc-finger proteins of the classical Cys2His2 type are the most | + | 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== | ==About this Structure== | ||
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[[Category: Klug, A.]] | [[Category: Klug, A.]] | ||
[[Category: Lu, D.]] | [[Category: Lu, D.]] | ||
| - | [[Category: Searles, M | + | [[Category: Searles, M A.]] |
[[Category: MG]] | [[Category: MG]] | ||
[[Category: ZN]] | [[Category: ZN]] | ||
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[[Category: zinc finger]] | [[Category: zinc finger]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:26:23 2008'' |
Revision as of 13:26, 21 February 2008
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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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