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Structural and mechanistic insights provided by single particle cryo-EM analysis of phosphoinositide 3-kinase (PI3Kα).
Vogt, Peter K; Hart, Jonathan R; Yang, Su; Zhou, Qingtong; Yang, Dehua; Wang, Ming-Wei.
Affiliation
  • Vogt PK; Department of Molecular Medicine, The Scripps Research Institute, La Jolla, CA 92037, United States of America. Electronic address: pkvogt@scripps.edu.
  • Hart JR; Department of Molecular Medicine, The Scripps Research Institute, La Jolla, CA 92037, United States of America.
  • Yang S; Department of Molecular Medicine, The Scripps Research Institute, La Jolla, CA 92037, United States of America.
  • Zhou Q; Department of Pharmacology, School of Basic Medical Sciences, Fudan University, Shanghai 200032, China.
  • Yang D; The National Center for Drug Screening, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai 201203, China.
  • Wang MW; Department of Pharmacology, School of Basic Medical Sciences, Fudan University, Shanghai 200032, China; Research Center for Deepsea Bioresources, Sanya 572025, China; Department of Chemistry, School of Science, The University of Tokyo, Tokyo 113-0033, Japan.
Biochim Biophys Acta Rev Cancer ; 1878(5): 188947, 2023 09.
Article in En | MEDLINE | ID: mdl-37394020
ABSTRACT
Recent cryo-electron microscopic (cryo-EM) investigations have succeeded in the analysis of various structural conformations and functional states of PI3Kα, a dimer consisting of the catalytic subunit p110α and the regulatory subunit p85α of class IA of phosphoinositide 3-kinase. High resolution structures have been obtained of the unliganded and of BYL-719-bound PI3Kα. The latter provides information on excessively flexible domains of p85α that are then further analyzed with nanobodies and CXMS (chemical cross-linking, digestion and mass spectrometry). Analysis of p110α helical and kinase domain mutations reveals mutant-specific features that can be linked to the gain of function in enzymatic and signaling activities.
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Phosphatidylinositol 3-Kinases / Phosphatidylinositol 3-Kinase Limits: Humans Language: En Journal: Biochim Biophys Acta Rev Cancer Year: 2023 Document type: Article
Fulltext
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Phosphatidylinositol 3-Kinases / Phosphatidylinositol 3-Kinase Limits: Humans Language: En Journal: Biochim Biophys Acta Rev Cancer Year: 2023 Document type: Article