1j4w | pdb_00001j4w
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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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
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