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| <StructureSection load='' size='350' side='right' scene='' caption='Human CREB-binding protein with acetyllysine complex with SCN- and K+ (purple) ions [[3p1c]]'> | | <StructureSection load='3p1c' size='350' side='right' scene='54/541099/Cv/1' 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]]]]
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| == Function == | | == Function == |
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Revision as of 13:36, 31 January 2016
| 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
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3D Structures of CREB-binding protein
Updated on 31-January-2016
{"openlevels":0}
- CBP
- 4i9o – mCBP GACKIX domain (mutant) - mouse
- 1f81 – mCBP TAZ2 domain - NMR
- 1u2n – mCBP TAZ1 domain - NMR
- 1jjs – mCBP IBiD domain - NMR
- 1liq – mCBP CH1 domain - NMR
- 1tot – mCBP ZZ domain – NMR
- 2kkj – mCBP nuclear coactivator binding domain - NMR
- 1wo3, 1wo4, 1wo5, 1wo6, 1wo7 – hCBP zinc finger domain (mutant) – human - NMR
- 2d82 – hCBP bromodomain - NMR
- 3dwy – hCBP bromodomain
- 3p1c, 3p1d, 3p1e, 3p1f, 3svh, 4a9k – hCBP bromodomain + small molecule
- 2l84, 2l85 – hCBP bromodomain + small molecule - NMR
- CBP complex with protein
- 1kbh – hCBP + nuclear receptor coactivator - NMR
- 1zoq – hCBP + interferon regulatory factor 3
- 2c52 – mCBP residues 2059-2117 + nuclear receptor coactivator - NMR
- 1r8u – mCBP TAZ1 domain + P300-interacting transactivator - NMR
- 1l8c – mCBP TAZ1 domain + hypoxia-inducible factor 1α - NMR
- 2lww - mCBP TAZ1 domain + nuclear transcription factor RELA – NMR
- 2ka6 – mCBP TAZ2 domain + STAT1-TAD - NMR
- 2ka4 – mCBP TAZ2 domain + STAT2-TAD - NMR
- 1kdx – mCBP KIX domain + CREB kinase inducible domain - NMR
- 2kje – hCBP TAZ2 domain + adenoviral E1A peptide - NMR
- 1jsp – hCBP bromodomain + p53 peptide - NMR
- 2l14 – mCBP nuclear coactivator binding domain + p53 peptide - NMR
- 1sb0 – mCBP KIX domain + protein c-Myb – NMR
- 2agh – mCBP KIX domain + protein c-Myb + zinc finger protein HRX – NMR
- 2lqh, 2lqi – mCBP KIX domain + forkhead box O3 – NMR
- 2kwf – hCBP KIX domain + transcription factor 4 – NMR
- 2lxs, 2lxt – hCBP KIX domain + histone methyltransferase MLL peptide – NMR
- 2rny – hCBP bromodomain + histone H3 peptide - NMR
- 4n3w, 4n4f - hCBP bromodomain + histone H4 peptide
- 4nr4, 4nr5, 4nr6, 4nr7, 4nyv, 4nyw, 4nyx- hCBP bromodomain + ligand
References
