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Modulation of allostery by protein intrinsic disorder

Author

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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
    Skaggs Institute for Chemical Biology, 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)

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).

Suggested Citation

  • Allan Chris M. Ferreon & Josephine C. Ferreon & Peter E. Wright & Ashok A. Deniz, 2013. "Modulation of allostery by protein intrinsic disorder," Nature, Nature, vol. 498(7454), pages 390-394, June.
  • Handle: RePEc:nat:nature:v:498:y:2013:i:7454:d:10.1038_nature12294
    DOI: 10.1038/nature12294
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    Cited by:

    1. Zhihong Xiao & Jinyin Zha & Xu Yang & Tingting Huang & Shuxin Huang & Qi Liu & Xiaozheng Wang & Jie Zhong & Jianting Zheng & Rubing Liang & Zixin Deng & Jian Zhang & Shuangjun Lin & Shaobo Dai, 2024. "A three-level regulatory mechanism of the aldo-keto reductase subfamily AKR12D," Nature Communications, Nature, vol. 15(1), pages 1-15, December.

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