Ontology highlight
ABSTRACT:
SUBMITTER: Schalk-Hihi C
PROVIDER: S-EPMC3081545 | biostudies-literature | 2011 Apr
REPOSITORIES: biostudies-literature
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]