1un6

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|PDB= 1un6 |SIZE=350|CAPTION= <scene name='initialview01'>1un6</scene>, resolution 3.10&Aring;
|PDB= 1un6 |SIZE=350|CAPTION= <scene name='initialview01'>1un6</scene>, resolution 3.10&Aring;
|SITE= <scene name='pdbsite=BN4:Zn-Binding+Site'>BN4</scene>
|SITE= <scene name='pdbsite=BN4:Zn-Binding+Site'>BN4</scene>
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|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> and <scene name='pdbligand=MG:MAGNESIUM ION'>MG</scene>
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|LIGAND= <scene name='pdbligand=A:ADENOSINE-5&#39;-MONOPHOSPHATE'>A</scene>, <scene name='pdbligand=C:CYTIDINE-5&#39;-MONOPHOSPHATE'>C</scene>, <scene name='pdbligand=G:GUANOSINE-5&#39;-MONOPHOSPHATE'>G</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=U:URIDINE-5&#39;-MONOPHOSPHATE'>U</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
|ACTIVITY=
|ACTIVITY=
|GENE=
|GENE=
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|DOMAIN=
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|RELATEDENTRY=
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|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.]]
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[[Category: MG]]
 
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[[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]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:34:21 2008''
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''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


PDB ID 1un6

Drag the structure with the mouse to rotate
, resolution 3.10Å
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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