CREB-binding protein
From Proteopedia
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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/ | + | <scene name='54/541099/Cv/5'>Acetyllysine binding site</scene> with chain A. Water molecules are shown as red spheres. |
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| + | <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]] | ||
| - | + | </StructureSection> | |
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| - | **[[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 /> | ||
| - | **[[2n1a]] – hCBP + small ubiquitin-related modifier - NMR<br /> | ||
| - | **[[5jem]] – hCBP residues 2065-2111 + interferon-3<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]] | ||
Current revision
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References
- ↑ 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
- ↑ 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
- ↑ 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
