1un6
From Proteopedia
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|PDB= 1un6 |SIZE=350|CAPTION= <scene name='initialview01'>1un6</scene>, resolution 3.10Å | |PDB= 1un6 |SIZE=350|CAPTION= <scene name='initialview01'>1un6</scene>, resolution 3.10Å | ||
|SITE= <scene name='pdbsite=BN4:Zn-Binding+Site'>BN4</scene> | |SITE= <scene name='pdbsite=BN4:Zn-Binding+Site'>BN4</scene> | ||
- | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=A:ADENOSINE-5'-MONOPHOSPHATE'>A</scene>, <scene name='pdbligand=C:CYTIDINE-5'-MONOPHOSPHATE'>C</scene>, <scene name='pdbligand=G:GUANOSINE-5'-MONOPHOSPHATE'>G</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=U:URIDINE-5'-MONOPHOSPHATE'>U</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
+ | |DOMAIN= | ||
+ | |RELATEDENTRY= | ||
+ | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1un6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1un6 OCA], [http://www.ebi.ac.uk/pdbsum/1un6 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1un6 RCSB]</span> | ||
}} | }} | ||
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[[Category: Lu, D.]] | [[Category: Lu, D.]] | ||
[[Category: Searles, M A.]] | [[Category: Searles, M A.]] | ||
- | [[Category: MG]] | ||
- | [[Category: ZN]] | ||
[[Category: 5s ribosomal rna]] | [[Category: 5s ribosomal rna]] | ||
[[Category: dna-binding]] | [[Category: dna-binding]] | ||
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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 Mon Mar 31 00:12:35 2008'' |
Revision as of 21:12, 30 March 2008
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, resolution 3.10Å | |||||||
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Sites: | |||||||
Ligands: | , , , , , | ||||||
Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
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. The following page contains interesting information on the relation of 1UN6 with [Zinc Fingers]. 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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