Distortion of a cellobio-derived isofagomine highlights the potential conformational itinerary of inverting beta-glucosidases.

Autor: Varrot A; Structural Biology Laboratory, Department of Chemistry, The University of York, Heslington, York, UK Y010 5YW., Macdonald J, Stick RV, Pell G, Gilbert HJ, Davies GJ
Jazyk: angličtina
Zdroj: Chemical communications (Cambridge, England) [Chem Commun (Camb)] 2003 Apr 21 (8), pp. 946-7.
DOI: 10.1039/b301592k
Abstrakt: A cellobio-derived isofagomine glycosidase inhibitor (Ki approximately 400 nM) displays an unusual distorted 2,5B (boat) conformation upon binding to cellobiohydrolase Cel6A from Humicola insolens, highlighting the different conformational itineraries used by various glycosidases, with consequences for the design of therapeutic agents.
Databáze: MEDLINE