Summary: Creb binding
This is the Wikipedia entry entitled "Creb binding domain". More...
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Creb binding domain Edit Wikipedia article
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In molecular biology, the creb binding domain is a protein domain. It is the interlocking domain of the eukaryotic nuclear receptor coactivators CREBBP and P300. This interlocking domain forms a 3-helical non-globular array that forms interlocked heterodimers with its target.
Nuclear receptors are ligand-activated transcription factors involved in the regulation of many processes, including development, reproduction and homeostasis. Nuclear receptor coactivators act to modulate the function of nuclear receptors. Coactivators associate with promoters and enhancers primarily through protein-protein contacts to facilitate the interaction between DNA-bound transcription factors and the transcription machinery. Many of these coactivators are structurally related, including CBP (CREB-binding protein, CREBBP) and P300. CBP and P300 both have histone acetyltransferase activity. CBP/P300 proteins function synergistically to activate transcription, acting to remodel chromatin and to recruit RNA polymerase II and the basal transcription machinery. CBP is required for proper cell cycle control, differentiation and apoptosis. The interaction of CBP/P300 with transcription factors involves several small domains. The IBiD domain in the C-terminal of CBP is responsible for CBP interaction with IRF-3, as well as with the adenoviral oncoprotein E1A, TIF-2 coactivator, and the IRF homologue KSHV IRF-1.
- Demarest SJ, Martinez-Yamout M, Chung J, Chen H, Xu W, Dyson HJ, Evans RM, Wright PE (January 2002). "Mutual synergistic folding in recruitment of CBP/p300 by p160 nuclear receptor coactivators". Nature 415 (6871): 54953. DOI:10.1038/415549a. PMID 11823864.
- Lin CH, Hare BJ, Wagner G, Harrison SC, Maniatis T, Fraenkel E (September 2001). "A small domain of CBP/p300 binds diverse proteins: solution structure and functional studies". Mol. Cell 8 (3): 58190. DOI:10.1016/S1097-2765(01)00333-1. PMID 11583620.
Creb binding Provide feedback
The Creb binding domain assumes a structure comprising of three alpha-helices which pack in a bundle, exposing a hydrophobic groove between alpha-1 and alpha-3 within which complimentary domains found in the protein 'activator for thyroid hormone and retinoid receptors' (ACTR) can dock. Docking of these domains is required for the recruitment of RNA polymerase II and the basal transcription machinery .
Demarest SJ, Martinez-Yamout M, Chung J, Chen H, Xu W, Dyson HJ, Evans RM, Wright PE; , Nature. 2002;415:549-553.: Mutual synergistic folding in recruitment of CBP/p300 by p160 nuclear receptor coactivators. PUBMED:11823864 EPMC:11823864
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR014744
This entry represents the interlocking domain of the eukaryotic nuclear receptor coactivators CREBP and p300. The interlocking domain forms a 3-helical non-globular array that forms interlocked heterodimers with its target.
Nuclear receptors are ligand-activated transcription factors involved in the regulation of many processes, including development, reproduction and homeostasis. Nuclear receptor coactivators act to modulate the function of nuclear receptors. Coactivators associate with promoters and enhancers primarily through protein-protein contacts to facilitate the interaction between DNA-bound transcription factors and the transcription machinery. Many of these coactivators are structurally related, including CBP (CREB-binding protein) and p300 [PUBMED:11823864]. CBP and p300 both have histone acetyltransferase activity (EC). CBP/p300 proteins function synergistically to activate transcription, acting to remodel chromatin and to recruit RNA polymerase II and the basal transcription machinery. CBP is required for proper cell cycle control, differentiation and apoptosis. The interaction of CBP/p300 with transcription factors involves several small domains. The IBiD domain in the C-terminal of CBP is responsible for CBP interaction with IRF-3, as well as with the adenoviral oncoprotein E1A, TIF-2 coactivator, and the IRF homologue KSHV IRF-1 [PUBMED:11583620].
|Cellular component||nucleus (GO:0005634)|
|histone acetyltransferase complex (GO:0000123)|
|Molecular function||transcription coactivator activity (GO:0003713)|
|histone acetyltransferase activity (GO:0004402)|
|Biological process||regulation of transcription, DNA-dependent (GO:0006355)|
|histone acetylation (GO:0016573)|
- the number of sequences which exhibit this architecture
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This example describes an architecture with one
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EGFdomains, and finally a single
- the UniProt description of the protein sequence
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Curation and family details
|Author:||Mistry J, Sammut SJ|
|Number in seed:||4|
|Number in full:||148|
|Average length of the domain:||105.30 aa|
|Average identity of full alignment:||55 %|
|Average coverage of the sequence by the domain:||4.94 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||5|
|Download:||download the raw HMM for this family|
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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Creb_binding domain has been found. There are 7 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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