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CREB-binding protein

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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.
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<scene name='54/541099/Cv/4'>Acetyllysine binding site</scene> with chain A.
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<scene name='54/541099/Cv/2'>Acetyllysine binding site</scene> with chain B.
</StructureSection>
</StructureSection>
== 3D Structures of CREB-binding protein ==
== 3D Structures of CREB-binding protein ==

Revision as of 14:03, 31 January 2016

Human CREB-binding protein with acetyllysine complex with SCN- and K+ (purple) ions 3p1c

Drag the structure with the mouse to rotate

3D Structures of CREB-binding protein

Updated on 31-January-2016

References

  1. ↑ 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:http://dx.doi.org/10.1038/365855a0
  2. ↑ 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:http://dx.doi.org/10.1038/376348a0

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