Ontology highlight
ABSTRACT:
SUBMITTER: Tyukhtenko S
PROVIDER: S-EPMC5789057 | biostudies-literature | 2018 Jan
REPOSITORIES: biostudies-literature
Tyukhtenko Sergiy S Rajarshi Girija G Karageorgos Ioannis I Zvonok Nikolai N Gallagher Elyssia S ES Huang Hongwei H Vemuri Kiran K Hudgens Jeffrey W JW Ma Xiaoyu X Nasr Mahmoud L ML Pavlopoulos Spiro S Makriyannis Alexandros A
Scientific reports 20180129 1
An understanding of how conformational dynamics modulates function and catalysis of human monoacylglycerol lipase (hMGL), an important pharmaceutical target, can facilitate the development of novel ligands with potential therapeutic value. Here, we report the discovery and characterization of an allosteric, regulatory hMGL site comprised of residues Trp-289 and Leu-232 that reside over 18 Å away from the catalytic triad. These residues were identified as critical mediators of long-range communic ...[more]