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Maeda, Shoji; Koehl, Antoine; Matile, Hugues; Hu, Hongli; Hilger, Daniel; Schertler, Gebhard F X; Manglik, Aashish; Skiniotis, Georgios; Dawson, Roger J P; Kobilka, Brian K
Nature communications, 09/2018, Letnik: 9, Številka: 1Journal Article
Single-particle cryo-electron microscopy (cryo-EM) has recently enabled high-resolution structure determination of numerous biological macromolecular complexes. Despite this progress, the application of high-resolution cryo-EM to G protein coupled receptors (GPCRs) in complex with heterotrimeric G proteins remains challenging, owning to both the relative small size and the limited stability of these assemblies. Here we describe the development of antibody fragments that bind and stabilize GPCR-G protein complexes for the application of high-resolution cryo-EM. One antibody in particular, mAb16, stabilizes GPCR/G-protein complexes by recognizing an interface between Gα and Gβγ subunits in the heterotrimer, and confers resistance to GTPγS-triggered dissociation. The unique recognition mode of this antibody makes it possible to transfer its binding and stabilizing effect to other G-protein subtypes through minimal protein engineering. This antibody fragment is thus a broadly applicable tool for structural studies of GPCR/G-protein complexes.
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JCR | SNIP | JCR | SNIP | JCR | SNIP | JCR | SNIP |
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