Modelling of the mechanism of covalent adduct formation by the inhibitor O-arylcarbamate URB524 in FAAH shows that only one of the two possible inhibitor binding orientations is consistent with the experimentally observed irreversible carbamoylation of the nucleophile serine: this is a potentially crucial insight for designing new covalent inhibitors of this promising drug target.
Identification of productive inhibitor binding orientation in fatty acid amide hydrolase (FAAH) by QM/MM mechanistic modelling / Lodola, Alessio; Mor, Marco; Rivara, Silvia; Christov, C.; Tarzia, G.; Piomelli, D.; Mulholland, A. J.. - In: CHEMICAL COMMUNICATIONS. - ISSN 1359-7345. - (2008), pp. 214-216. [10.1039/B714136J]
Identification of productive inhibitor binding orientation in fatty acid amide hydrolase (FAAH) by QM/MM mechanistic modelling.
LODOLA, Alessio;MOR, Marco;RIVARA, Silvia;
2008-01-01
Abstract
Modelling of the mechanism of covalent adduct formation by the inhibitor O-arylcarbamate URB524 in FAAH shows that only one of the two possible inhibitor binding orientations is consistent with the experimentally observed irreversible carbamoylation of the nucleophile serine: this is a potentially crucial insight for designing new covalent inhibitors of this promising drug target.| File | Dimensione | Formato | |
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