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J. Biol. Chem., Vol. 281, Issue 21, 14787-14795, May 26, 2006

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Structural Diversity in p160/CREB-binding Protein Coactivator Complexes^*

Lorna Waters¹², Baigong Yue², Vaclav Veverka, Philip Renshaw, Janice Bramham, Sachiko Matsuda, Thomas Frenkiel^¶, Geoffrey Kelly^¶, Frederick Muskett, Mark Carr, Supported by Wellcome Trust Grants 066047 and 063632³, and David M. Heery⁴

From the Department of Biochemistry, Henry Wellcome Building, University of Leicester, Lancaster Road, Leicester LE1 9HN, United Kingdom, School of Pharmacy, University of Nottingham, University Park, Nottingham NG7 2RD, United Kingdom, and ^¶Medical Research Council Biomedical NMR Centre, National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, United Kingdom

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 (C1, C2, C3, and C3' in CBP and S1, S2', S2, and S3 in SRC1). A tight four-helix bundle is formed between S1, C1, C2, and C3 that is capped by S3. In contrast to the structure of the AD1 domain of the related p160 protein ACTR in complex with CBP SID, the sequences forming S2' and S2 in SRC1 AD1 are not involved in the interface between the two domains but rather serve to position S3. 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.

Received for publication, January 10, 2006 , and in revised form, March 14, 2006.

The atomic coordinates and structure factors (code 2C52) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

^* This work was supported in part by Grant 054401/Z/98/B from the Wellcome Trust (to D. M. H.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ Supported by a Ph.D. studentship from the Biotechnology and Biological Sciences Research Council.

² Both authors should be considered as equal first authors.

³ To whom correspondence may be addressed: Dept. of Biochemistry, Henry Wellcome Bldg., University of Leicester, Lancaster Rd., Leicester LE1 9HN, UK. Tel.: 44-116-229-7075; Fax: 44-116-229-7018; E-mail: mdc12{at}le.ac.uk. ⁴ To whom correspondence may be addressed: School of Pharmacy, University of Nottingham, University Park, Nottingham NG7 2RD, UK. Tel.: 44-115-951-5087; Fax: 44-115-846-6249; E-mail: david.heery{at}nottingham.ac.uk.

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