CREB-binding protein: Difference between revisions

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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.


<scene name='54/541099/Cv/4'>Acetyllysine binding site</scene> with chain A. Water molecules are shown as red spheres.
<scene name='54/541099/Cv/5'>Acetyllysine binding site</scene> with chain A. Water molecules are shown as red spheres.


<scene name='54/541099/Cv/2'>Acetyllysine binding site</scene> with chain B ([[3p1c]]).<ref>PMID:22464331</ref>
<scene name='54/541099/Cv/6'>Acetyllysine binding site</scene> with chain B ([[3p1c]]).<ref>PMID:22464331</ref>
</StructureSection>
</StructureSection>
== 3D Structures of CREB-binding protein ==
== 3D Structures of CREB-binding protein ==

Revision as of 09:56, 18 February 2019

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.

with chain A. Water molecules are shown as red spheres.

with chain B (3p1c).[3]

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 protein3D Structures of CREB-binding protein

Updated on 18-February-2019

ReferencesReferences

  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
  3. Filippakopoulos P, Picaud S, Mangos M, Keates T, Lambert JP, Barsyte-Lovejoy D, Felletar I, Volkmer R, Muller S, Pawson T, Gingras AC, Arrowsmith CH, Knapp S. Histone recognition and large-scale structural analysis of the human bromodomain family. Cell. 2012 Mar 30;149(1):214-31. PMID:22464331 doi:10.1016/j.cell.2012.02.013

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky