Ontology highlight
ABSTRACT:
SUBMITTER: Manthei KA
PROVIDER: S-EPMC6277198 | biostudies-literature | 2018 Nov
REPOSITORIES: biostudies-literature
Manthei Kelly A KA Yang Shyh-Ming SM Baljinnyam Bolormaa B Chang Louise L Glukhova Alisa A Yuan Wenmin W Freeman Lita A LA Maloney David J DJ Schwendeman Anna A Remaley Alan T AT Jadhav Ajit A Tesmer John Jg JJ
eLife 20181127
Lecithin:cholesterol acyltransferase (LCAT) and LCAT-activating compounds are being investigated as treatments for coronary heart disease (CHD) and familial LCAT deficiency (FLD). Herein we report the crystal structure of human LCAT in complex with a potent piperidinylpyrazolopyridine activator and an acyl intermediate-like inhibitor, revealing LCAT in an active conformation. Unlike other LCAT activators, the piperidinylpyrazolopyridine activator binds exclusively to the membrane-binding domain ...[more]