Modulation of allostery by protein intrinsic disorder

被引：0
|
作者：
Allan Chris M. Ferreon
Josephine C. Ferreon
Peter E. Wright
Ashok A. Deniz
机构：
[1] The Scripps Research Institute,Department of Integrative Structural and Computational Biology
[2] 10550 North Torrey Pines Road,undefined
[3] La Jolla,undefined
[4] California 92037,undefined
[5] USA,undefined
[6] Skaggs Institute for Chemical Biology,undefined
[7] The Scripps Research Institute,undefined
[8] 10550 North Torrey Pines Road,undefined
[9] La Jolla,undefined
[10] California 92037,undefined
[11] USA,undefined
来源：
Nature | 2013年 / 498卷
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摘要：
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).
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页码：390 / 394
页数：4
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