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Structure of the GPCR dimer Ste2 bound to an antagonist


ABSTRACT:

SUBMITTER: Christopher Gordon Tate 

PROVIDER: EMPIAR-10877 | biostudies-other |

REPOSITORIES: biostudies-other

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Activation mechanism of the class D fungal GPCR dimer Ste2.

Velazhahan Vaithish V   Ma Ning N   Vaidehi Nagarajan N   Tate Christopher G CG  

Nature 20220316 7902


The fungal class D1 G-protein-coupled receptor (GPCR) Ste2 has a different arrangement of transmembrane helices compared with mammalian GPCRs and a distinct mode of coupling to the heterotrimeric G protein Gpa1-Ste2-Ste18<sup>1</sup>. In addition, Ste2 lacks conserved sequence motifs such as DRY, PIF and NPXXY, which are associated with the activation of class A GPCRs<sup>2</sup>. This suggested that the activation mechanism of Ste2 may also differ. Here we determined structures of Saccharomyces  ...[more]

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