Cryo-electron microscopy structure of the P-Rex1–G-beta-gamma signaling scaffold
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ABSTRACT:
SUBMITTER: Michael Cianfrocco
PROVIDER: EMPIAR-10285 | biostudies-other |
REPOSITORIES: biostudies-other
Publications
Cryo-electron microscopy structure and analysis of the P-Rex1-Gβγ signaling scaffold.
Cash Jennifer N JN Urata Sarah S Li Sheng S Ravala Sandeep K SK Avramova Larisa V LV Shost Michael D MD Gutkind J Silvio JS Tesmer John J G JJG Cianfrocco Michael A MA
Science advances 20191016 10
PIP<sub>3</sub>-dependent Rac exchanger 1 (P-Rex1) is activated downstream of G protein-coupled receptors to promote neutrophil migration and metastasis. The structure of more than half of the enzyme and its regulatory G protein binding site are unknown. Our 3.2 Å cryo-EM structure of the P-Rex1-Gβγ complex reveals that the carboxyl-terminal half of P-Rex1 adopts a complex fold most similar to those of <i>Legionella</i> phosphoinositide phosphatases. Although catalytically inert, the domain coal ...[more]
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