Modulation of allostery by protein intrinsic disorder

Allan Chris M. Ferreon, Josephine C. Ferreon, Peter E. Wright () and Ashok A. Deniz ()
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Allan Chris M. Ferreon: The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037, USA
Josephine C. Ferreon: The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037, USA
Peter E. Wright: The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037, USA
Ashok A. Deniz: The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037, USA

Nature, 2013, vol. 498, issue 7454, 390-394

Abstract: Single-molecule FRET is used to examine how an intrinsically disordered protein, the adenovirus E1A oncoprotein, interacts with two different protein partners (the pocket domain of pRb and the TAZ2 domain of CBP/p300); the biophysical behaviour of E1A depends on whether the N-terminal region and/or the CR2 region of E1A is free to interact with potential protein partners or whether they are ‘masked’ (that is, via their absence or a pre-existing interaction with another protein partner).

Date: 2013
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DOI: 10.1038/nature12294

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