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8JQG

Cryo EM map of full length PLC gamma 2

Summary for 8JQG
Entry DOI10.2210/pdb8jqg/pdb
EMDB information36571
Descriptor1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-2 (1 entity in total)
Functional Keywordsplcg2, plc gamma 2, hydrolase
Biological sourceHomo sapiens (human)
Total number of polymer chains1
Total formula weight148074.58
Authors
Shin, Y.-C.,Liao, M. (deposition date: 2023-06-14, release date: 2024-12-11)
Primary citationShin, Y.C.,Plummer-Medeiros, A.M.,Mungenast, A.,Choi, H.W.,TenDyke, K.,Zhu, X.,Shepard, J.,Sanders, K.,Zhuang, N.,Hu, L.,Qian, D.,Song, K.,Xu, C.,Wang, J.,Poda, S.B.,Liao, M.,Chen, Y.
The crystal and cryo-EM structures of PLC gamma 2 reveal dynamic interdomain recognitions in autoinhibition.
Sci Adv, 10:eadn6037-eadn6037, 2024
Cited by
PubMed Abstract: 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.
PubMed: 39612343
DOI: 10.1126/sciadv.adn6037
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.72 Å)
Structure validation

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건을2024-12-18부터공개중

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