<StructureSection load='' size='350' side='right' scene='' caption='Human CREB-binding protein with acetyllysine complex with SCN- and K+ (purple) ions [[3p1c]]'>
[[Image:1kbh.png|left|200px|thumb|Crystal structure of CREB-binding protein bromodomain (green) complex with nuclear receptor coactivator (grey) [[1kbh]]]]
[[Image:1kbh.png|left|200px|thumb|Crystal structure of CREB-binding protein bromodomain (green) complex with nuclear receptor coactivator (grey) [[1kbh]]]]
{{STRUCTURE_3p1c| PDB=3p1c | SIZE=350| SCENE= |right|CAPTION=Human CREB-binding protein with acetyllysine complex with SCN- and K+ (purple) ions [[3p1c]] }}
== Function ==
== Function ==
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CBP contains several domains. Among them the lysine recognition bromodomain; domains KIX, TAZ1 and TAZ2 which bind sequences spanning the transactivation domain of transcription factor p53; IBiD which binds the interferon response; ZZ is a zinc-binding motif; CH1 (Cys- and His-rich region 1) interacts with the N-terminal of p73.
CBP contains several domains. Among them the lysine recognition bromodomain; domains KIX, TAZ1 and TAZ2 which bind sequences spanning the transactivation domain of transcription factor p53; IBiD which binds the interferon response; ZZ is a zinc-binding motif; CH1 (Cys- and His-rich region 1) interacts with the N-terminal of p73.
</StructureSection>
== 3D Structures of CREB-binding protein ==
== 3D Structures of CREB-binding protein ==
Revision as of 13:33, 31 January 2016
Human CREB-binding protein with acetyllysine complex with SCN- and K+ (purple) ions 3p1c
File:1kbh.pngCrystal structure of CREB-binding protein bromodomain (green) complex with nuclear receptor coactivator (grey) 1kbh
Function
CREB-binding protein (CBP) is a transcription activator. CREB is cAMP response element-binding protein which is a cellular transcription factor which binds to DNA and regulates transcription. CBP acetylates histones. It binds to phosphorylated CREB and enhances its activity. [1]
Disease
Mutations in CBP cause Rubinstein-Taybi syndrome.[2]
Structural highlights
CBP contains several domains. Among them the lysine recognition bromodomain; domains KIX, TAZ1 and TAZ2 which bind sequences spanning the transactivation domain of transcription factor p53; IBiD which binds the interferon response; ZZ is a zinc-binding motif; CH1 (Cys- and His-rich region 1) interacts with the N-terminal of p73.
↑Chrivia JC, Kwok RP, Lamb N, Hagiwara M, Montminy MR, Goodman RH. Phosphorylated CREB binds specifically to the nuclear protein CBP. Nature. 1993 Oct 28;365(6449):855-9. PMID:8413673 doi:https://dx.doi.org/10.1038/365855a0
↑Petrij F, Giles RH, Dauwerse HG, Saris JJ, Hennekam RC, Masuno M, Tommerup N, van Ommen GJ, Goodman RH, Peters DJ, et al.. Rubinstein-Taybi syndrome caused by mutations in the transcriptional co-activator CBP. Nature. 1995 Jul 27;376(6538):348-51. PMID:7630403 doi:https://dx.doi.org/10.1038/376348a0