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J. Biol. Chem., Vol. 280, Issue 7, 5682-5692, February 18, 2005
Biochemical and NMR Mapping of the Interface between CREB-binding Protein and Ligand Binding Domains of Nuclear ReceptorBEYOND THE LXXLL MOTIF*![]() ![]() ![]() ![]() ||
From the
CBP, cAMP-response element-binding protein (CREB)-binding protein, plays an important role as a general cointegrator of various signaling pathways and interacts with a large number of transcription factors. Interactions of CBP with ligand binding domains (LBDs) of nuclear receptors are mediated by LXXLL motifs, as are those of p160 proteins, although the number, distribution, and precise sequences of the motifs differ. We used a large N-terminal fragment of murine CBP to map by biochemical methods and NMR spectroscopy the interaction domain of CBP with the LBDs of several nuclear receptors. We show that distinct zones of that fragment are involved in the interactions: a 20-residue segment containing the LXXLL motif (residues 6180) is implicated in the interaction with all three domains tested (peroxisome proliferator-activated receptor
Received for publication, October 14, 2004 , and in revised form, November 10, 2004. * This work was supported by the CNRS, INSERM, Université Louis Pasteur (Strasbourg), and by funds from the Genopôle Alsace-Lorraine and the European Commission as SPINE, Contract QLG2-CT-2002-00988 under the Public Research, Technology, and Development program Quality of Life and Management of Living Resources. 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.
|| To whom correspondence should be addressed. Tel.: 33-03-8865-3256; Fax: 33-03-8865-3276; E-mail: cava{at}igbmc.u-strasbg.fr.
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