Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Structures of the PI3Kα/KRas complex on lipid bilayers reveal molecular mechanisms of PI3Kα activation.
Journal, issue, pages	Mol Cell, Vol. 86, Issue 14, Page 2858-22870.e6, Year 2026
Publish date	Jul 16, 2026
Authors	Hayarpi Torosyan / Michael D Paul / Brigitte G Meyer / Allison Maker / Natalia Jura / Kliment A Verba /
PubMed Abstract	PI3Kα is a potent oncogene that converts PIP2 to PIP3 at the plasma membrane upon activation by receptor tyrosine kinases and Ras. To understand the molecular mechanism of PI3Kα activation, we used ...PI3Kα is a potent oncogene that converts PIP2 to PIP3 at the plasma membrane upon activation by receptor tyrosine kinases and Ras. To understand the molecular mechanism of PI3Kα activation, we used cryo-electron microscopy to visualize the conformational states that underlie its transition to an active signaling complex. Here, we present structures of the PI3Kα/KRas complex embedded in lipid nanodiscs, revealing a rich ensemble of PI3Kα conformations that capture the progressive release of key inhibitory domains from the PI3Kα catalytic core. PIP2 triggers significant restructuring of active site regulatory motifs while an activating phosphopeptide induces dimerization of the PI3Kα/KRas complex through a p110α catalytic subunit-mediated interface that is sterically occluded in autoinhibited PI3Kα. In cells, dimeric PI3Kα amplifies Akt signaling in response to growth factor stimulation. Collectively, these structures map the conformational landscape of PI3Kα activation and reveal previously unexplored interfaces for potential therapeutic targeting.
External links	Mol Cell / PubMed:42349404
Methods	EM (single particle)
Resolution	2.61 - 10.0 Å
Structure data	49451 9ni3 EMDB-49451, PDB-9ni3: Cryo-EM structure of the PI3K alpha/KRas complex on POPC/POPS/PIP2 nanodiscs Method: EM (single particle) / Resolution: 2.82 Å 49452 9ni4 EMDB-49452, PDB-9ni4: Cryo-EM structure of the PI3K alpha/KRas/HER3 phosphopeptide complex dimer on POPC/POPS/PIP2 nanodiscs Method: EM (single particle) / Resolution: 2.61 Å 49453 9ni5 EMDB-49453, PDB-9ni5: Cryo-EM structure of the PI3K alpha/KRas/HER3 phosphopeptide complex on POPC/POPS/PIP2 nanodiscs Method: EM (single particle) / Resolution: 2.89 Å 49454 9ni6 EMDB-49454, PDB-9ni6: Cryo-EM structure of the Class 1 PI3K alpha/KRas complex on POPC/POPS nanodiscs Method: EM (single particle) / Resolution: 3.01 Å 49455 9ni7 EMDB-49455, PDB-9ni7: Cryo-EM structure of the Class 3 PI3K alpha/KRas complex on POPC/POPS nanodiscs Method: EM (single particle) / Resolution: 3.05 Å 49456 9ni8 EMDB-49456, PDB-9ni8: Cryo-EM structure of the Class 2 PI3K alpha/KRas complex on POPC/POPS nanodiscs Method: EM (single particle) / Resolution: 3.23 Å 49458 9nid EMDB-49458, PDB-9nid: Cryo-EM structure of the PI3K alpha/KRas/HER3 phosphopeptide complex dimer on POPC/POPS/PIP2 nanodiscs low-pass filtered to 5 angstroms Method: EM (single particle) / Resolution: 5.0 Å 49459 9nie EMDB-49459, PDB-9nie: Cryo-EM structure of the PI3K alpha/KRas/HER3 phosphopeptide complex on POPC/POPS/PIP2 nanodiscs low-pass filtered to 5 angstroms Method: EM (single particle) / Resolution: 5.0 Å 49460 9nif EMDB-49460, PDB-9nif: Cryo-EM structure of the PI3K alpha/KRas complex on POPC/POPS/PIP2 nanodiscs low-pass filtered to 5 angstroms Method: EM (single particle) / Resolution: 5.0 Å 49519 9nlc EMDB-49519, PDB-9nlc: Cryo-EM structure of the Class 1 PI3K alpha/KRas complex on POPC/POPS nanodiscs low-pass filtered to 10 angstroms Method: EM (single particle) / Resolution: 10.0 Å
Chemicals	ChemComp-PBU: (2R)-3-{[(R)-HYDROXY{[(1R,2R,3S,4R,5R,6S)-2,3,6-TRIHYDROXY-4,5-BIS(PHOSPHONOOXY)CYCLOHEXYL]OXY}PHOSPHORYL]OXY}PROPANE-1 PDB-1azd: CONCANAVALIN FROM CANAVALIA BRASILIENSIS ChemComp-MG: Unknown entry ChemComp-GNP: PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER / GppNHp, GMPPNP, energy-carrying molecule analogue*YM
Source	homo sapiens (human)
Keywords	ONCOPROTEIN/Hydrolase / lipid kinase / GTPase / ONCOPROTEIN / ONCOPROTEIN-Hydrolase complex / Transferase/Hydrolase / Transferase-Hydrolase complex