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http://hdl.handle.net/2445/125313
Title: | Active site-directed inhibitors of prolyl oligopeptidase abolishes its conformational dynamics |
Author: | López, Abraham Herranz-Trillo, F. Kotev, Martin Gairí Tahull, Margarida Guallar, Victor Bernadó Peretó, Pau Millet Aguilar-Galindo, Òscar Tarragó Clua, Maria Teresa Giralt Lledó, Ernest |
Keywords: | Espectroscòpia de ressonància magnètica nuclear Proteïnes Nuclear magnetic resonance spectroscopy Proteins |
Issue Date: | 2016 |
Publisher: | Wiley-VCH |
Abstract: | Deciphering conformational dynamics is crucial for understanding the biological functions of proteins and for designing compounds targeting them. In particular, providing an accurate description of microsecond-millisecond motions opens the opportunity for regulating protein-protein interactions (PPIs) by modulating the dynamics of one interacting partner. Here we analyzed the conformational dynamics of prolyl oligopeptidase (POP) and the effects of active-site-directed inhibitors on the dynamics. We used an integrated structural biology approach based on NMR spectroscopy and SAXS experiments complemented by MD simulations. We found that POP is in a slow equilibrium in solution between open and closed conformations, and that inhibitors effectively abolished this equilibrium by stabilizing the enzyme in the closed conformation. |
Note: | Versió postprint del document publicat a: https://doi.org/10.1002/cbic.201600102 |
It is part of: | ChemBioChem, 2016, vol. 17, num. 10, p. 913-917 |
URI: | http://hdl.handle.net/2445/125313 |
Related resource: | https://doi.org/10.1002/cbic.201600102 |
ISSN: | 1439-4227 |
Appears in Collections: | Articles publicats en revistes (Química Inorgànica i Orgànica) |
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