1997
DOI: 10.1016/s0092-8674(00)80463-8
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Solution Structure of the KIX Domain of CBP Bound to the Transactivation Domain of CREB: A Model for Activator:Coactivator Interactions

Abstract: The nuclear factor CREB activates transcription of target genes in part through direct interactions with the KIX domain of the coactivator CBP in a phosphorylation-dependent manner. The solution structure of the complex formed by the phosphorylated kinase-inducible domain (pKID) of CREB with KIX reveals that pKID undergoes a coil-->helix folding transition upon binding to KIX, forming two alpha helices. The amphipathic helix alphaB of pKID interacts with a hydrophobic groove defined by helices alpha1 and alpha… Show more

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Cited by 702 publications
(998 citation statements)
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“…6). More generally, the fold of Med25 ACID is unique amongst known activator target domains 21,[45][46][47] such as Tfb1, Mdm2, PAS-B and the CBP KIX domain, which are all unrelated in structure (Fig. 6).…”
Section: Discussionmentioning
confidence: 99%
“…6). More generally, the fold of Med25 ACID is unique amongst known activator target domains 21,[45][46][47] such as Tfb1, Mdm2, PAS-B and the CBP KIX domain, which are all unrelated in structure (Fig. 6).…”
Section: Discussionmentioning
confidence: 99%
“…One protein that follows the folding after binding pathway is the pKID of the transcription factor CREB. pKID exists as an unfolded protein in solution in vitro (Radhakrishnan et al 1997) but folds upon binding to the KIX domain of the CREB binding protein (Parker et al 1996). The structure of the pKID-KIX complex has been solved by NMR (Radhakrishnan et al 1997), revealing that the pKID forms two helices and that the C-terminal helix in particular is very well-defined, interacting specifically with KIX (Fig.…”
Section: Coupled Folding/bindingmentioning
confidence: 99%
“…Since the interaction between MBF1 and FTZ-F1 is rather stable, it is implied that the N-terminal residues undergo folding transitions when they encounters the activator. Induced folding from otherwise unfolded states is often encountered in protein-protein interactions between transcriptional factors: the activation domain of p53 by binding to MDM2 (Kussie et al 1996), the activation domain of VP16 by binding to hTAF II 31 (Uesugi et al 1997), KIX domain by binding to CBP (Radhakrishnan et al 1997), and the transcriptional inhibitory domain of dTAF II 230 by binding to TBP (Liu et al 1998). MBF1 is characterized by its ability to bind several different transcriptional factors, for instance: human MBF1 can bind to either Ad4BP, ATF1, CREB1 or CREBP1 (Y. Kabe, M. Goto, D. Shima, T. Wada, K. Morohashi, M. Shirakawa, S. Hirose & H. Handa, unpublished result).…”
Section: The N-terminal Residuesmentioning
confidence: 99%