Cryo-EM structures of human arachidonate 12S-lipoxygenase bound to endogenous and exogenous inhibitors

• Published in: Blood Vol. 142; no. 14; pp. 1233 - 1242
• Main Authors: Mobbs, Jesse I., Black, Katrina A., Tran, Michelle, Burger, Wessel A. C., Venugopal, Hariprasad, Holman, Theodore R., Holinstat, Michael, Thal, David M., Glukhova, Alisa
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 05.10.2023; The American Society of Hematology
• Subjects: Arachidonate 12-Lipoxygenase - metabolism; Arachidonic Acid - metabolism; Cryoelectron Microscopy; Humans; Platelet Activation; Platelets and Thrombopoiesis; Thrombocytopenia; United States; United States

•The first full-length structure of human arachidonate 12-LOX reveal mechanisms of its oligomeric and conformational states.•The structures uncover the natural inhibitor of 12-LOX and reveal the binding site of inhibitor ML355. [Display omitted] Human 12-lipoxygenase (12-LOX) is a key enzyme involve...