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A new side opening on prolyl oligopeptidase revealed by electron microscopy
Author(s) -
Tarragó Teresa,
Martín-Benito Jaime,
Sabidó Eduard,
Claasen Birgit,
Madurga Sergio,
Gairí Margarida,
Valpuesta José M.,
Giralt Ernest
Publication year - 2009
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2009.09.036
Subject(s) - oligopeptidase , electron microscope , side chain , triad (sociology) , chemistry , nuclear magnetic resonance , psychology , physics , biochemistry , enzyme , optics , polymer , psychoanalysis
Prolyl oligopeptidase (POP) has gained importance as a target for the treatment of neuropsychiatric diseases and cognitive disturbances. Therefore, a variety of strategies are currently used to identify POP inhibitors. Here we performed electron microscopy (EM) studies of human POP. Our data reveal for the first time the presence of a new side opening in POP that was not observed in any of the crystallographic structures described to date. Finally, molecular dynamics, the relevant normal modes that contribute to the fluctuation of the catalytic triad residues and the algorithm CAVERN also support the existence of a new large side opening on POP.