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Peng JW. Investigating Dynamic Interdomain Allostery in Pin1. Biophys Rev. 2015;7(2):239-249doi: 10.1007/s12551-015-0171-9.
Peng, J. W. (2015). Investigating Dynamic Interdomain Allostery in Pin1. Biophysical reviews, 7(2), 239-249. https://doi.org/10.1007/s12551-015-0171-9
Peng, Jeffrey W. "Investigating Dynamic Interdomain Allostery in Pin1." Biophysical reviews vol. 7,2 (2015): 239-249. doi: https://doi.org/10.1007/s12551-015-0171-9
Peng JW. Investigating Dynamic Interdomain Allostery in Pin1. Biophys Rev. 2015 Jun 01;7(2):239-249. doi: 10.1007/s12551-015-0171-9. Epub 2015 Apr 22. PMID: 26495045; PMCID: PMC4610412.
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Biophys Rev. 2015 Jun 01;7(2):239-249. doi: 10.1007/s12551-015-0171-9. Epub 2015 Apr 22.

Investigating Dynamic Interdomain Allostery in Pin1.

Biophysical reviews

Jeffrey W Peng

Affiliations

  1. Department of Chemistry and Biochemistry, University of Notre Dame, 251 Nieuwland Science Hall, Notre Dame, IN 46556.

PMID: 26495045 PMCID: PMC4610412 DOI: 10.1007/s12551-015-0171-9

Abstract

Signaling proteins often sequester complementary functional sites in separate domains. How do the different domains communicate with one another? An attractive system to address this question is the mitotic regulator, human Pin1 (Lu et al. 1996). Pin-1 consists of two tethered domains: a WW domain for substrate binding, and a catalytic domain for peptidyl-prolyl isomerase (PPIase) activity. Pin1 accelerates the cis-trans isomerization of phospho-Ser/Thr-Pro (pS/T-P) motifs within proteins regulating the cell cycle and neuronal development. The early x-ray (Ranganathan et al. 1997; Verdecia et al. 2000) and solution NMR studies (Bayer et al. 2003; Jacobs et al. 2003) of Pin1 indicated inter- and intradomain motion. We became interested in exploring how such motions might affect interdomain communication, using NMR. Our accumulated results indicate substrate binding to Pin1 WW domain changes the intra/inter domain mobility, thereby altering substrate activity in the distal PPIase domain catalytic site. Thus, Pin1 shows evidence of dynamic allostery, in the sense of Cooper and Dryden (Cooper and Dryden 1984). We highlight our results supporting this conclusion, and summarize them via a simple speculative model of conformational selection.

Keywords: IDR; NMR; PPIase; Pin1; WW domain; allostery; correlated motion; protein dynamics

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