Structure of the GPCR dimer Ste2 bound to an antagonist
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ABSTRACT:
SUBMITTER: Christopher Gordon Tate
PROVIDER: EMPIAR-10877 | biostudies-other |
REPOSITORIES: biostudies-other
Publications
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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