Description
Experimental Technique/Method:SOLUTION NMR
Resolution:
Classification:TRANSCRIPTION REGULATION COMPLEX
Release Date:1998-11-25
Deposition Date:1997-09-16
Revision Date:2008-03-24#2011-07-13
Molecular Weight:12942.55
Macromolecule Type:Protein
Residue Count:109
Atom Site Count:907
DOI:10.2210/pdb1kdx/pdb
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 alpha3 of KIX. The other pKID helix, alphaA, contacts a different face of the alpha3 helix. The phosphate group of the critical phosphoserine residue of pKID forms a hydrogen bond to the side chain of Tyr-658 of KIX. The structure provides a model for interactions between other transactivation domains and their targets.
Resolution:
Classification:TRANSCRIPTION REGULATION COMPLEX
Release Date:1998-11-25
Deposition Date:1997-09-16
Revision Date:2008-03-24#2011-07-13
Molecular Weight:12942.55
Macromolecule Type:Protein
Residue Count:109
Atom Site Count:907
DOI:10.2210/pdb1kdx/pdb
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 alpha3 of KIX. The other pKID helix, alphaA, contacts a different face of the alpha3 helix. The phosphate group of the critical phosphoserine residue of pKID forms a hydrogen bond to the side chain of Tyr-658 of KIX. The structure provides a model for interactions between other transactivation domains and their targets.
Date made available | 1998 |
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Publisher | RCSB-PDB |