A structural basis for how ligand binding site changes can allosterically regulate GPCR signaling and engender functional selectivity | Zendy

Marta SánchezSoto | Zendy; Ravi Kumar Verma | Zendy; Blair K. A. Willette | Zendy; Elizabeth C. Gonye | Zendy; Annah M. Moore | Zendy; Amy E. Moritz | Zendy; Comfort A. Boateng | Zendy; Hideaki Yano | Zendy; R. Benjamin Free | Zendy; Lei Shi | Zendy; David R. Sibley | Zendy

Open Access

A structural basis for how ligand binding site changes can allosterically regulate GPCR signaling and engender functional selectivity

Author(s) -

Marta SánchezSoto,

Ravi Kumar Verma,

Blair K. A. Willette,

Elizabeth C. Gonye,

Annah M. Moore,

Amy E. Moritz,

Comfort A. Boateng,

Hideaki Yano,

R. Benjamin Free,

Lei Shi,

David R. Sibley

Publication year - 2020

Publication title -

science signaling

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 3.659

H-Index - 154

eISSN - 1937-9145

pISSN - 1945-0877

DOI - 10.1126/scisignal.aaw5885

Subject(s) - g protein coupled receptor , functional selectivity , arrestin , microbiology and biotechnology , transmembrane domain , intracellular , agonist , signal transduction , biology , receptor , allosteric regulation , biophysics , ligand (biochemistry) , g protein , chemistry , biochemistry

A conserved amino acid residue in the ligand binding site of class A GPCRs regulates receptor interactions with β-arrestin.

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