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1KDX

KIX DOMAIN OF MOUSE CBP (CREB BINDING PROTEIN) IN COMPLEX WITH PHOSPHORYLATED KINASE INDUCIBLE DOMAIN (PKID) OF RAT CREB (CYCLIC AMP RESPONSE ELEMENT BINDING PROTEIN), NMR 17 STRUCTURES

Summary for 1KDX
Entry DOI10.2210/pdb1kdx/pdb
DescriptorCBP, CREB (2 entities in total)
Functional Keywordscomplex (transcription activator-co-activator), protein-protein interaction, phosphoserine recognition, transcription regulation complex
Biological sourceMus musculus (house mouse)
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Cellular locationCytoplasm (By similarity): P45481
Nucleus: P15337
Total number of polymer chains2
Total formula weight12942.56
Authors
Radhakrishnan, I.,Perez-Alvarado, G.C.,Dyson, H.J.,Wright, P.E. (deposition date: 1997-09-16, release date: 1998-11-25, Last modification date: 2024-11-06)
Primary citationRadhakrishnan, I.,Perez-Alvarado, G.C.,Parker, D.,Dyson, H.J.,Montminy, M.R.,Wright, P.E.
Solution structure of the KIX domain of CBP bound to the transactivation domain of CREB: a model for activator:coactivator interactions.
Cell(Cambridge,Mass.), 91:741-752, 1997
Cited by
PubMed 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.
PubMed: 9413984
DOI: 10.1016/S0092-8674(00)80463-8
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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