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CREB-binding protein
From Proteopedia
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| - | + | <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]]'> | |
| - | + | == Function == | |
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| + | '''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 == | ||
| + | Mutations in CBP cause Rubinstein-Taybi syndrome.<ref>PMID:7630403</ref> | ||
| + | == 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. | ||
| + | <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> | |
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== 3D Structures of CREB-binding protein == | == 3D Structures of CREB-binding protein == | ||
| + | [[CREB-binding protein 3D structures]] | ||
| - | + | </StructureSection> | |
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| + | == 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
