Ontology highlight
ABSTRACT:
SUBMITTER: Bowling FZ
PROVIDER: S-EPMC7117805 | biostudies-literature | 2020 Apr
REPOSITORIES: biostudies-literature
Bowling Forrest Z FZ Salazar Christian M CM Bell Justin A JA Huq Tahrima S TS Frohman Michael A MA Airola Michael V MV
Nature chemical biology 20200316 4
The signal transduction enzyme phospholipase D1 (PLD1) hydrolyzes phosphatidylcholine to generate the lipid second-messenger phosphatidic acid, which plays roles in disease processes such as thrombosis and cancer. PLD1 is directly and synergistically regulated by protein kinase C, Arf and Rho GTPases, and the membrane lipid phosphatidylinositol-4,5-bisphosphate (PIP<sub>2</sub>). Here, we present a 1.8 Å-resolution crystal structure of the human PLD1 catalytic domain, which is characterized by a ...[more]