磷酸肌醇3激酶
蛋白质亚单位
P110α
二聚体
低温电子显微
化学
突变体
单粒子分析
结构生物学
生物物理学
PI3K/AKT/mTOR通路
计算生物学
细胞生物学
生物化学
信号转导
生物
基因
有机化学
气溶胶
作者
Peter K. Vogt,Jonathan R. Hart,Yang Su,Qingtong Zhou,Dehua Yang,Mingwei Wang
标识
DOI:10.1016/j.bbcan.2023.188947
摘要
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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