2C52

Structural diversity in CBP p160 complexes

Summary for 2C52

• Entry DOI: 10.2210/pdb2c52/pdb
• Related: 1F81 1JJS 1KBH 1KDX 1L8C 1R8U 1SB0 1TOT 1U2N 1XIU 2A3I
• NMR Information: BMRB: 6874
• Descriptor: CREB-BINDING PROTEIN, NUCLEAR RECEPTOR COACTIVATOR 1 (2 entities in total)
• Functional Keywords: transferase, activator, bromodomain, metal-binding, methylation, nuclear protein, transcription, transcription regulation, zinc, zinc-finger, acyltransferase, alternative splicing, chromosomal translocation, polymorphism, proto-oncogene, ubl conjugation
• Biological source: MUS MUSCULUS (MOUSE); More
• Cellular location: Cytoplasm : P45481
• Total number of polymer chains: 2
• Total formula weight: 12867.68

Authors

Waters, L.C.,Yue, B.,Veverka, V.,Renshaw, P.S.,Bramham, J.,Matsuda, S.,Frenkiel, T.,Kelly, G.,Muskett, F.W.,Carr, M.D.,Heery, D.M. (deposition date: 2005-10-25, release date: 2006-03-15, Last modification date: 2024-05-15)

Primary citation

Waters, L.,Yue, B.,Veverka, V.,Renshaw, P.,Bramham, J.,Matsuda, S.,Frenkiel, T.,Kelly, G.,Muskett, F.,Carr, M.,Heery, D.M.
Structural diversity in p160/CREB-binding protein coactivator complexes.
J. Biol. Chem., 281:14787-14795, 2006

PubMed Abstract: 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.

PubMed: 16540468
DOI: 10.1074/jbc.M600237200

Experimental method

SOLUTION NMR