Detailed biophysical and biochemical studies provide an exquisite example of how conformational flexibility controls the interaction between an intrinsically disordered protein and its numerous binding partners.
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References
Eliezer, D. Curr. Opin. Struct. Biol. 19, 23–30 (2009).
Dyson, H.J. & Wright, P.E. Nat. Rev. Mol. Cell Biol. 6, 197–208 (2005).
Wright, P.E. & Dyson, H.J. Curr. Opin. Struct. Biol. 19, 31–38 (2009).
Dunker, A.K. et al. BMC Genomics 9 Suppl 2, S1 (2008).
Mittag, T. & Forman-Kay, J.D. Curr. Opin. Struct. Biol. 17, 3–14 (2007).
Tompa, P. Structure and Function of Intrinsically Disordered Proteins, 331 (Taylor and Francis Group, Boca Raton, 2010).
Daughdrill, G.W., Pielak, G.J., Uversky, V.N., Cortese, M.S. & Dunker, A.K. Natively disordered proteins. in Protein Folding Handbook, Vol. 3 (eds. Buchner, J. & Kiefhaber, T.) 275–357 (Wiley-VCH, Darmstadt, 2005).
Xiong, Y. et al. Nature 366, 701–704 (1993).
Wang, Y. et al. Nat. Chem. Biol. 7, 214–221 (2011).
Russo, A.A., Jeffrey, P.D., Patten, A.K., Massague, J. & Pavletich, N.P. Nature 382, 325–331 (1996).
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Daughdrill, G. Bridging the gap. Nat Chem Biol 7, 193–194 (2011). https://doi.org/10.1038/nchembio.544
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DOI: https://doi.org/10.1038/nchembio.544