1un6
From Proteopedia
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==Overview== | ==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 . | + | 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== | ||
| - | 1UN6 is a | + | 1UN6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis] with ZN and MG as [http://en.wikipedia.org/wiki/ligands ligands]. The following page contains interesting information on the relation of 1UN6 with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb87_1.html Zinc Fingers]]. Structure known Active Site: BN4. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1UN6 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: zinc finger]] | [[Category: zinc finger]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 14:28:44 2007'' |
Revision as of 12:23, 5 November 2007
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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 ZN and MG as ligands. The following page contains interesting information on the relation of 1UN6 with [Zinc Fingers]. Structure known Active Site: BN4. 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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