2c52: Difference between revisions
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|ACTIVITY= [http://en.wikipedia.org/wiki/Histone_acetyltransferase Histone acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.48 2.3.1.48] | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Histone_acetyltransferase Histone acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.48 2.3.1.48] </span> | ||
|GENE= | |GENE= | ||
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2c52 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c52 OCA], [http://www.ebi.ac.uk/pdbsum/2c52 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2c52 RCSB]</span> | |||
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[[Category: zinc-finger]] | [[Category: zinc-finger]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:16:26 2008'' | ||
Revision as of 02:16, 31 March 2008
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| Activity: | Histone acetyltransferase, with EC number 2.3.1.48 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURAL DIVERSITY IN CBP P160 COMPLEXES
OverviewOverview
Ligand-induced transcription by nuclear receptors involves the recruitment of p160 coactivators such as steroid receptor coactivator 1 (SRC1), in complex with histone acetyltransferases such as CREB-binding protein (CBP) and p300. Here we describe the solution structure of a complex formed by the SRC1 interaction domain (SID) of CBP and the activation domain (AD1) of SRC1, both of which contain four helical regions (Calpha1, Calpha2, Calpha3, and Calpha3' in CBP and Salpha1, Salpha2', Salpha2, and Salpha3 in SRC1). A tight four-helix bundle is formed between Salpha1, Calpha1, Calpha2, and Calpha3 that is capped by Salpha3. In contrast to the structure of the AD1 domain of the related p160 protein ACTR in complex with CBP SID, the sequences forming Salpha2' and Salpha2 in SRC1 AD1 are not involved in the interface between the two domains but rather serve to position Salpha3. Thus, although the CBP SID domain adopts a similar fold in complex with different p160 proteins, the topologies of the AD1 domains are strikingly different, a feature that is likely to contribute to functional specificity of these coactivator complexes.
About this StructureAbout this Structure
2C52 is a Protein complex structure of sequences from Homo sapiens and Mus musculus. Full crystallographic information is available from OCA.
ReferenceReference
Structural diversity in p160/CREB-binding protein coactivator complexes., Waters L, Yue B, Veverka V, Renshaw P, Bramham J, Matsuda S, Frenkiel T, Kelly G, Muskett F, Carr M, Heery DM, J Biol Chem. 2006 May 26;281(21):14787-95. Epub 2006 Mar 15. PMID:16540468
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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCA- Pages with broken file links
- Histone acetyltransferase
- Homo sapiens
- Mus musculus
- Protein complex
- Bramham, J.
- Carr, M D.
- Frenkiel, T.
- Heery, D M.
- Kelly, G.
- Matsuda, S.
- Muskett, F W.
- Renshaw, P S.
- Veverka, V.
- Waters, L C.
- Yue, B.
- Activator
- Acyltransferase
- Alternative splicing
- Bromodomain
- Chromosomal translocation
- Metal-binding
- Methylation
- Nuclear protein
- Polymorphism
- Proto-oncogene
- Transcription
- Transcription regulation
- Transferase
- Ubl conjugation
- Zinc
- Zinc-finger