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-Structure paper
タイトル | The crystal and cryo-EM structures of PLCγ2 reveal dynamic interdomain recognitions in autoinhibition. |
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ジャーナル・号・ページ | Sci Adv, Vol. 10, Issue 48, Page eadn6037, Year 2024 |
掲載日 | 2024年11月29日 |
![]() | Young-Cheul Shin / Ashlee Marie Plummer-Medeiros / Alison Mungenast / Hyeong-Wook Choi / Karen TenDyke / Xiaojie Zhu / Jennifer Shepard / Kristen Sanders / Ningning Zhuang / Liang Hu / Dongming Qian / Kangkang Song / Chen Xu / John Wang / Suresh B Poda / Maofu Liao / Yu Chen / ![]() ![]() |
PubMed 要旨 | Phospholipase C gamma 2 (PLCγ2) plays important roles in cell signaling downstream of various membrane receptors. PLCγ2 contains a multidomain inhibitory region critical for its regulation, while ...Phospholipase C gamma 2 (PLCγ2) plays important roles in cell signaling downstream of various membrane receptors. PLCγ2 contains a multidomain inhibitory region critical for its regulation, while it has remained unclear how these domains contribute to PLCγ2 activity modulation. Here we determined three structures of human PLCγ2 in autoinhibited states, which reveal dynamic interactions at the autoinhibition interface, involving the conformational flexibility of the Src homology 3 (SH3) domain in the inhibitory region, and its previously unknown interaction with a carboxyl-terminal helical domain in the core region. We also determined a structure of PLCγ2 bound to the kinase domain of fibroblast growth factor receptor 1 (FGFR1), which demonstrates the recognition of FGFR1 by the nSH2 domain in the inhibitory region of PLCγ2. Our results provide structural insights into PLCγ2 regulation that will facilitate future mechanistic studies to understand the entire activation process. |
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手法 | EM (単粒子) / X線回折 |
解像度 | 2.55 - 4.2 Å |
構造データ | EMDB-36571, PDB-8jqg: EMDB-36572, PDB-8jqh: EMDB-36573, PDB-8jqi: ![]() PDB-8t7c: |
化合物 | ![]() ChemComp-CA: ![]() ChemComp-EDO: ![]() ChemComp-HOH: |
由来 |
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![]() | HYDROLASE / PLCg2 / PLC gamma 2 / Phospholipase C gamma 2 / autoinhibition / signaling / lipid metabolism |