PMID- 16540468 OWN - NLM STAT- MEDLINE DCOM- 20060707 LR - 20220129 IS - 0021-9258 (Print) IS - 0021-9258 (Linking) VI - 281 IP - 21 DP - 2006 May 26 TI - Structural diversity in p160/CREB-binding protein coactivator complexes. PG - 14787-95 AB - 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. FAU - Waters, Lorna AU - Waters L AD - Department of Biochemistry, Henry Wellcome Building, University of Leicester, Lancaster Road, Leicester LE1 9HN, United Kingdom. FAU - Yue, Baigong AU - Yue B FAU - Veverka, Vaclav AU - Veverka V FAU - Renshaw, Philip AU - Renshaw P FAU - Bramham, Janice AU - Bramham J FAU - Matsuda, Sachiko AU - Matsuda S FAU - Frenkiel, Thomas AU - Frenkiel T FAU - Kelly, Geoffrey AU - Kelly G FAU - Muskett, Frederick AU - Muskett F FAU - Carr, Mark AU - Carr M FAU - Heery, David M AU - Heery DM LA - eng SI - PDB/2C52 GR - MC_U117533887/MRC_/Medical Research Council/United Kingdom GR - 063632/WT_/Wellcome Trust/United Kingdom GR - 066047/WT_/Wellcome Trust/United Kingdom GR - 054401/Z/98/B/WT_/Wellcome Trust/United Kingdom PT - Journal Article PT - Research Support, Non-U.S. Gov't DEP - 20060315 PL - United States TA - J Biol Chem JT - The Journal of biological chemistry JID - 2985121R RN - 0 (DNA-Binding Proteins) RN - 0 (MYBBP1A protein, human) RN - 0 (Nuclear Proteins) RN - 0 (Nucleocytoplasmic Transport Proteins) RN - 0 (RNA-Binding Proteins) RN - 0 (Transcription Factors) RN - EC 2.3.1.48 (CREB-Binding Protein) RN - EC 2.3.1.48 (Histone Acetyltransferases) RN - EC 2.3.1.48 (NCOA1 protein, human) RN - EC 2.3.1.48 (Ncoa1 protein, mouse) RN - EC 2.3.1.48 (Nuclear Receptor Coactivator 1) SB - IM MH - Amino Acid Sequence MH - Animals MH - CREB-Binding Protein/*chemistry MH - DNA-Binding Proteins MH - Histone Acetyltransferases MH - Humans MH - Mice MH - Models, Molecular MH - Molecular Conformation MH - Molecular Sequence Data MH - Nuclear Proteins/chemistry MH - Nuclear Receptor Coactivator 1 MH - Nucleocytoplasmic Transport Proteins/chemistry MH - Protein Binding MH - Protein Conformation MH - Protein Structure, Tertiary MH - RNA-Binding Proteins MH - Sequence Homology, Amino Acid MH - Transcription Factors/chemistry EDAT- 2006/03/17 09:00 MHDA- 2006/07/11 09:00 CRDT- 2006/03/17 09:00 PHST- 2006/03/17 09:00 [pubmed] PHST- 2006/07/11 09:00 [medline] PHST- 2006/03/17 09:00 [entrez] AID - S0021-9258(20)72422-1 [pii] AID - 10.1074/jbc.M600237200 [doi] PST - ppublish SO - J Biol Chem. 2006 May 26;281(21):14787-95. doi: 10.1074/jbc.M600237200. Epub 2006 Mar 15.