CREB-binding protein: Difference between revisions

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== Function ==
== 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. <ref>PMID:8413673</ref>
'''CREB-binding protein''' or '''CREBBP''' (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. <ref>PMID:8413673</ref>


== Disease ==
== Disease ==
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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/6'>Acetyllysine binding site</scene> with chain B ([[3p1c]]).<ref>PMID:22464331</ref>


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


Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
</StructureSection>
{{#tree:id=OrganizedByTopic|openlevels=0|
 
*CBP
 
**[[4i9o]] – mCBP GACKIX domain (mutant) - mouse <br />
**[[1f81]] – mCBP TAZ2 domain - NMR <br />
**[[1u2n]] – mCBP TAZ1 domain - NMR <br />
**[[1jjs]] – mCBP IBiD domain - NMR<br />
**[[1liq]] – mCBP CH1 domain - NMR<br />
**[[1tot]] – mCBP ZZ domain – NMR <br />
**[[2kkj]] – mCBP nuclear coactivator binding domain - NMR <br />
**[[1wo3]], [[1wo4]], [[1wo5]], [[1wo6]], [[1wo7]] – hCBP zinc finger domain (mutant) – human - NMR <br />
**[[2d82]] – hCBP bromodomain  - NMR<br />
**[[3dwy]] – hCBP bromodomain  <br />
**[[3p1c]], [[3p1d]], [[3p1e]], [[3p1f]], [[3svh]], [[4a9k]] – hCBP bromodomain  + small molecule<br />
**[[2l84]], [[2l85]] – hCBP bromodomain  + small molecule - NMR<br />
 
*CBP complex with protein


**[[1kbh]] – hCBP + nuclear receptor coactivator - NMR <br />
**[[1zoq]] – hCBP + interferon regulatory factor 3  <br />
**[[2c52]] – mCBP residues 2059-2117 + nuclear receptor coactivator  - NMR<br />
**[[1r8u]] – mCBP TAZ1 domain + P300-interacting transactivator - NMR <br />
**[[1l8c]] – mCBP TAZ1 domain  + hypoxia-inducible factor 1α - NMR<br />
**[[2lww]] - mCBP TAZ1 domain  + nuclear transcription factor RELA – NMR <br />
**[[2ka6]] – mCBP TAZ2 domain  + STAT1-TAD - NMR<br />
**[[2ka4]] – mCBP TAZ2 domain  + STAT2-TAD - NMR<br />
**[[1kdx]] – mCBP KIX domain + CREB kinase inducible domain - NMR<br />
**[[2kje]] – hCBP TAZ2 domain  + adenoviral E1A peptide - NMR<br />
**[[1jsp]] – hCBP bromodomain  + p53 peptide - NMR<br />
**[[2l14]] – mCBP  nuclear coactivator binding domain + p53 peptide - NMR<br />
**[[1sb0]] – mCBP KIX domain + protein c-Myb – NMR <br />
**[[2agh]] – mCBP KIX domain + protein c-Myb + zinc finger protein HRX – NMR <br />
**[[2lqh]], [[2lqi]] – mCBP KIX domain + forkhead box O3 – NMR <br />
**[[2kwf]] – hCBP KIX domain + transcription factor 4 – NMR <br />
**[[2lxs]], [[2lxt]] – hCBP KIX domain + histone methyltransferase MLL peptide – NMR <br />
**[[2rny]] – hCBP bromodomain  + histone H3 peptide - NMR<br />
**[[4n3w]], [[4n4f]] - hCBP bromodomain  + histone H4 peptide <br />
**[[4nr4]], [[4nr5]], [[4nr6]], [[4nr7]], [[4nyv]], [[4nyw]], [[4nyx]]- hCBP bromodomain  + ligand<br />
}}
== References ==
== References ==
<references/>
<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Latest revision as of 12:28, 30 November 2022

Function

CREB-binding protein or CREBBP (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]

3D Structures of CREB-binding protein

CREB-binding protein 3D structures


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

Drag the structure with the mouse to rotate

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

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Michal Harel, Alexander Berchansky
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