Ontology highlight
ABSTRACT:
SUBMITTER: Schalk-Hihi C
PROVIDER: S-EPMC3081545 | biostudies-literature | 2011 Apr
REPOSITORIES: biostudies-literature
Schalk-Hihi Céline C Schubert Carsten C Alexander Richard R Bayoumy Shariff S Clemente Jose C JC Deckman Ingrid I DesJarlais Renee L RL Dzordzorme Keli C KC Flores Christopher M CM Grasberger Bruce B Kranz James K JK Lewandowski Frank F Liu Li L Ma Hongchang H Maguire Diane D Macielag Mark J MJ McDonnell Mark E ME Mezzasalma Haarlander Tara T Miller Robyn R Milligan Cindy C Reynolds Charles C Kuo Lawrence C LC
Protein science : a publication of the Protein Society 20110301 4
A high-resolution structure of a ligand-bound, soluble form of human monoglyceride lipase (MGL) is presented. The structure highlights a novel conformation of the regulatory lid-domain present in the lipase family as well as the binding mode of a pharmaceutically relevant reversible inhibitor. Analysis of the structure lacking the inhibitor indicates that the closed conformation can accommodate the native substrate 2-arachidonoyl glycerol. A model is proposed in which MGL undergoes conformationa ...[more]