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

Summary for 1J4W

• Entry DOI: 10.2210/pdb1j4w/pdb
• Descriptor: DNA (5'-D(*GP*TP*A*TP*AP*TP*TP*CP*CP*CP*TP*CP*GP*GP*G*AP*TP*TP*TP*TP*TP*TP*AP*TP*TP*TP*TP*GP*T)-3'), FUSE binding protein (2 entities in total)
• Functional Keywords: single-stranded dna binding protein, transcription factor, fbp, fuse element, c-myc oncogene, transcription-dna complex, transcription/dna
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus (Probable): Q96AE4
• Total number of polymer chains: 2
• Total formula weight: 27515.90

Authors

Clore, G.M.,Braddock, D.T. (deposition date: 2001-11-30, release date: 2002-03-06, Last modification date: 2023-12-27)

Primary citation

Braddock, D.T.,Louis, J.M.,Baber, J.L.,Levens, D.,Clore, G.M.
Structure and dynamics of KH domains from FBP bound to single-stranded DNA.
Nature, 415:1051-1056, 2002

PubMed Abstract: 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.

PubMed: 11875576
DOI: 10.1038/4151051a

Experimental method

SOLUTION NMR