Mechanism of coupled folding and binding of an intrinsically disordered protein
10.1038/nature05858
Crossref journal-article
Springer Science and Business Media LLC
Nature (297)
Bibliography

Sugase, K., Dyson, H. J., & Wright, P. E. (2007). Mechanism of coupled folding and binding of an intrinsically disordered protein. Nature, 447(7147), 1021–1025.

Authors 3
  1. Kenji Sugase (first)
  2. H. Jane Dyson (additional)
  3. Peter E. Wright (additional)
References 33 Referenced 939
  1. Tsai, C. J., Kumar, S., Ma, B. Y. & Nussinov, R. Folding funnels, binding funnels, and protein function. Protein Sci. 8, 1181–1190 (1999) (10.1110/ps.8.6.1181) / Protein Sci. by CJ Tsai (1999)
  2. Levy, Y., Cho, S. S., Onuchic, J. N. & Wolynes, P. G. A survey of flexible protein binding mechanisms and their transition states using native topology based energy landscapes. J. Mol. Biol. 346, 1121–1145 (2005) (10.1016/j.jmb.2004.12.021) / J. Mol. Biol. by Y Levy (2005)
  3. Wright, P. E. & Dyson, H. J. Intrinsically unstructured proteins: Re-assessing the protein structure-function paradigm. J. Mol. Biol. 293, 321–331 (1999) (10.1006/jmbi.1999.3110) / J. Mol. Biol. by PE Wright (1999)
  4. Dyson, H. J. & Wright, P. E. Coupling of folding and binding for unstructured proteins. Curr. Opin. Struct. Biol. 12, 54–60 (2002) (10.1016/S0959-440X(02)00289-0) / Curr. Opin. Struct. Biol. by HJ Dyson (2002)
  5. Dyson, H. J. & Wright, P. E. Intrinsically unstructured proteins and their functions. Nature Rev. Mol. Cell Biol. 6, 197–208 (2005) (10.1038/nrm1589) / Nature Rev. Mol. Cell Biol. by HJ Dyson (2005)
  6. Uversky, V. N. Natively unfolded proteins: A point where biology waits for physics. Protein Sci. 11, 739–756 (2002) (10.1110/ps.4210102) / Protein Sci. by VN Uversky (2002)
  7. Shoemaker, B. A., Portman, J. J. & Wolynes, P. G. Speeding molecular recognition by using the folding funnel: The fly-casting mechanism. Proc. Natl Acad. Sci. USA 97, 8868–8873 (2000) (10.1073/pnas.160259697) / Proc. Natl Acad. Sci. USA by BA Shoemaker (2000)
  8. Chrivia, J. C. et al. Phosphorylated CREB binds specifically to nuclear protein CBP. Nature 365, 855–859 (1993) (10.1038/365855a0) / Nature by JC Chrivia (1993)
  9. Kwok, R. P. S. et al. Nuclear protein CBP is a coactivator for the transcription factor CREB. Nature 370, 223–226 (1994) (10.1038/370223a0) / Nature by RPS Kwok (1994)
  10. Parker, D. et al. Phosphorylation of CREB at Ser133 induces complex formation with CPB via a direct mechanism. Mol. Cell. Biol. 16, 694–703 (1996) (10.1128/MCB.16.2.694) / Mol. Cell. Biol. by D Parker (1996)
  11. Radhakrishnan, I. et al. Solution structure of the KIX domain of CBP bound to the transactivation domain of CREB: A model for activator:coactivator interactions. Cell 91, 741–752 (1997) (10.1016/S0092-8674(00)80463-8) / Cell by I Radhakrishnan (1997)
  12. Shih, H. M. et al. A positive genetic selection for disrupting protein-protein interactions: Identification of CREB mutations that prevent association with the coactivator CBP. Proc. Natl Acad. Sci. USA 93, 13896–13901 (1996) (10.1073/pnas.93.24.13896) / Proc. Natl Acad. Sci. USA by HM Shih (1996)
  13. Shaywitz, A. J., Dove, S. L., Kornhauser, J. M., Hochschild, A. & Greenberg, M. E. Magnitude of the CREB-dependent transcriptional response is determined by the strength of the interaction between the kinase-inducible domain of CREB and the KIX domain of CREB-binding protein. Mol. Cell. Biol. 20, 9409–9422 (2000) (10.1128/MCB.20.24.9409-9422.2000) / Mol. Cell. Biol. by AJ Shaywitz (2000)
  14. Parker, D. et al. Analysis of an activator:coactivator complex reveals an essential role for secondary structure in transcriptional activation. Mol. Cell 2, 353–359 (1998) (10.1016/S1097-2765(00)80279-8) / Mol. Cell by D Parker (1998)
  15. Loria, J. P., Rance, M. & Palmer, A. G. A relaxation-compensated Carr-Purcell-Meiboom-Gill sequence for characterizing chemical exchange by NMR spectroscopy. J. Am. Chem. Soc. 121, 2331–2332 (1999) (10.1021/ja983961a) / J. Am. Chem. Soc. by JP Loria (1999)
  16. Mulder, F. A., Mittermaier, A., Hon, B., Dahlquist, F. W. & Kay, L. E. Studying excited states of proteins by NMR spectroscopy. Nature Struct. Biol. 8, 932–935 (2001) (10.1038/nsb1101-932) / Nature Struct. Biol. by FA Mulder (2001)
  17. Goto, N. K., Zor, T., Martinez-Yamout, M., Dyson, H. J. & Wright, P. E. Cooperativity in transcription factor binding to the coactivator CREB-binding protein (CBP). The mixed lineage leukemia protein (MLL) activation domain binds to an allosteric site on the KIX domain. J. Biol. Chem. 277, 43168–43174 (2002) (10.1074/jbc.M207660200) / J. Biol. Chem. by NK Goto (2002)
  18. De Guzman, R. N., Goto, N. K., Dyson, H. J. & Wright, P. E. Structural basis for cooperative transcription factor binding to the CBP coactivator. J. Mol. Biol. 355, 1005–1013 (2006) (10.1016/j.jmb.2005.09.059) / J. Mol. Biol. by RN De Guzman (2006)
  19. Gabdoulline, R. R. & Wade, R. C. Biomolecular diffusional association. Curr. Opin. Struct. Biol. 12, 204–213 (2002) (10.1016/S0959-440X(02)00311-1) / Curr. Opin. Struct. Biol. by RR Gabdoulline (2002)
  20. Berg, O. G. & von Hippel, P. H. Diffusion-controlled macromolecular interactions. Annu. Rev. Biophys. Biophys. Chem. 14, 131–160 (1985) (10.1146/annurev.bb.14.060185.001023) / Annu. Rev. Biophys. Biophys. Chem. by OG Berg (1985)
  21. Tang, C., Iwahara, J. & Clore, G. M. Visualization of transient encounter complexes in protein-protein association. Nature 444, 383–386 (2006) (10.1038/nature05201) / Nature by C Tang (2006)
  22. Volkov, A. N., Worrall, J. A. R., Holtzmann, E. & Ubbink, M. Solution structure and dynamics of the complex between cytochrome c and cytochrome c peroxidase determined by paramagnetic NMR. Proc. Natl Acad. Sci. USA 103, 18945–18950 (2006) (10.1073/pnas.0603551103) / Proc. Natl Acad. Sci. USA by AN Volkov (2006)
  23. Zor, T., De Guzman, R. N., Dyson, H. J. & Wright, P. E. Solution structure of the KIX domain of CBP bound to the transactivation domain of c-Myb. J. Mol. Biol. 337, 521–534 (2004) (10.1016/j.jmb.2004.01.038) / J. Mol. Biol. by T Zor (2004)
  24. Johnson, C. S. & Moreland, C. G. The calculation of NMR spectra for many-site exchange problems. J. Chem. Ed. 50, 477–483 (1973) (10.1021/ed050p477) / J. Chem. Ed. by CS Johnson (1973)
  25. Shoup, D. & Szabo, A. Role of diffusion in ligand binding to macromolecules and cell-bound receptors. Biophys. J. 40, 33–39 (1982) (10.1016/S0006-3495(82)84455-X) / Biophys. J. by D Shoup (1982)
  26. Selzer, T. & Schreiber, G. New insights into the mechanism of protein-protein association. Proteins Struct. Funct. Genet. 45, 190–198 (2001) (10.1002/prot.1139) / Proteins Struct. Funct. Genet. by T Selzer (2001)
  27. Tollinger, M., Skrynnikov, N. R., Mulder, F. A., Forman-Kay, J. D. & Kay, L. E. Slow dynamics in folded and unfolded states of an SH3 domain. J. Am. Chem. Soc. 123, 11341–11352 (2001) (10.1021/ja011300z) / J. Am. Chem. Soc. by M Tollinger (2001)
  28. McElheny, D., Schnell, J. R., Lansing, J. C., Dyson, H. J. & Wright, P. E. Defining the role of active-site loop fluctuations in dihydrofolate reductase catalysis. Proc. Natl Acad. Sci. USA 102, 5032–5037 (2005) (10.1073/pnas.0500699102) / Proc. Natl Acad. Sci. USA by D McElheny (2005)
  29. Koradi, R., Billeter, M. & Wüthrich, K. MOLMOL: A program for display and analysis of macromolecular structures. J. Mol. Graph. 14, 51–55 (1996) (10.1016/0263-7855(96)00009-4) / J. Mol. Graph. by R Koradi (1996)
  30. Huth, J. R. et al. Design of an expression system for detecting folded protein domains and mapping macromolecular interactions by NMR. Protein Sci. 6, 2359–2364 (1997) (10.1002/pro.5560061109) / Protein Sci. by JR Huth (1997)
  31. Grey, M. J., Wang, C. & Palmer, A. G. Disulfide bond isomerization in basic pancreatic trypsin inhibitor: Multisite chemical exchange quantified by CPMG relaxation dispersion and chemical shift modeling. J. Am. Chem. Soc. 125, 14324–14335 (2003) (10.1021/ja0367389) / J. Am. Chem. Soc. by MJ Grey (2003)
  32. Carver, J. P. & Richards, R. E. General 2-site solution for chemical exchange produced dependence of T2 upon Carr-Purcell pulse separation. J. Magn. Reson. 6, 89–105 (1972) / J. Magn. Reson. by JP Carver (1972)
  33. Allerhand, A. & Gutowsky, H. S. Spin-echo studies of chemical exchange. II. Closed formulas for two sites. J. Chem. Phys. 42, 1587–1599 (1965) (10.1063/1.1696165) / J. Chem. Phys. by A Allerhand (1965)
Dates
Type When
Created 18 years, 3 months ago (May 24, 2007, 7:44 a.m.)
Deposited 2 years, 3 months ago (May 18, 2023, 2:04 p.m.)
Indexed 6 days, 6 hours ago (Aug. 29, 2025, 6:19 a.m.)
Issued 18 years, 3 months ago (May 23, 2007)
Published 18 years, 3 months ago (May 23, 2007)
Published Online 18 years, 3 months ago (May 23, 2007)
Published Print 18 years, 3 months ago (June 1, 2007)
Funders 0

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@article{Sugase_2007, title={Mechanism of coupled folding and binding of an intrinsically disordered protein}, volume={447}, ISSN={1476-4687}, url={http://dx.doi.org/10.1038/nature05858}, DOI={10.1038/nature05858}, number={7147}, journal={Nature}, publisher={Springer Science and Business Media LLC}, author={Sugase, Kenji and Dyson, H. Jane and Wright, Peter E.}, year={2007}, month=may, pages={1021–1025} }