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1j4w

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[[Image:1j4w.gif|left|200px]]
[[Image:1j4w.gif|left|200px]]
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{{Structure
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|PDB= 1j4w |SIZE=350|CAPTION= <scene name='initialview01'>1j4w</scene>
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|LIGAND= <scene name='pdbligand=DA:2&#39;-DEOXYADENOSINE-5&#39;-MONOPHOSPHATE'>DA</scene>, <scene name='pdbligand=DC:2&#39;-DEOXYCYTIDINE-5&#39;-MONOPHOSPHATE'>DC</scene>, <scene name='pdbligand=DG:2&#39;-DEOXYGUANOSINE-5&#39;-MONOPHOSPHATE'>DG</scene>, <scene name='pdbligand=DT:THYMIDINE-5&#39;-MONOPHOSPHATE'>DT</scene>
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{{STRUCTURE_1j4w| PDB=1j4w | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1j4w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j4w OCA], [http://www.ebi.ac.uk/pdbsum/1j4w PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1j4w RCSB]</span>
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'''COMPLEX OF THE KH3 and KH4 DOMAINS OF FBP WITH A SINGLE_STRANDED 29mer DNA OLIGONUCLEOTIDE FROM THE FUSE ELEMENT OF THE C-MYC ONCOGENE'''
'''COMPLEX OF THE KH3 and KH4 DOMAINS OF FBP WITH A SINGLE_STRANDED 29mer DNA OLIGONUCLEOTIDE FROM THE FUSE ELEMENT OF THE C-MYC ONCOGENE'''
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[[Category: Braddock, D T.]]
[[Category: Braddock, D T.]]
[[Category: Clore, G M.]]
[[Category: Clore, G M.]]
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[[Category: c-myc oncogene]]
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[[Category: C-myc oncogene]]
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[[Category: fbp]]
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[[Category: Fbp]]
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[[Category: fuse element]]
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[[Category: Fuse element]]
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[[Category: single-stranded dna binding protein]]
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[[Category: Single-stranded dna binding protein]]
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[[Category: transcription factor]]
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[[Category: Transcription factor]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 20:48:32 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:28:52 2008''
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Revision as of 17:48, 2 May 2008

Template:STRUCTURE 1j4w

COMPLEX OF THE KH3 and KH4 DOMAINS OF FBP WITH A SINGLE_STRANDED 29mer DNA OLIGONUCLEOTIDE FROM THE FUSE ELEMENT OF THE C-MYC ONCOGENE


Overview

Gene regulation can be tightly controlled by recognition of DNA deformations that are induced by stress generated during transcription. The KH domains of the FUSE-binding protein (FBP), a regulator of c-myc expression, bind in vivo and in vitro to the single-stranded far-upstream element (FUSE), 1,500 base pairs upstream from the c-myc promoter. FBP bound to FUSE acts through TFIIH at the promoter. Here we report the solution structure of a complex between the KH3 and KH4 domains of FBP and a 29-base single-stranded DNA from FUSE. The KH domains recognize two sites, 9-10 bases in length, separated by 5 bases, with KH4 bound to the 5' site and KH3 to the 3' site. The central portion of each site comprises a tetrad of sequence 5'd-ATTC for KH4 and 5'd-TTTT for KH3. Dynamics measurements show that the two KH domains bind as articulated modules to single-stranded DNA, providing a flexible framework with which to recognize transient, moving targets.

About this Structure

1J4W is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structure and dynamics of KH domains from FBP bound to single-stranded DNA., Braddock DT, Louis JM, Baber JL, Levens D, Clore GM, Nature. 2002 Feb 28;415(6875):1051-6. PMID:11875576 Page seeded by OCA on Fri May 2 20:48:32 2008

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