Conserved Residues in the Gα interface show subtype specificity in Gβγ coupling

Abstract excerpt

Although the structural basis of selective G-protein coupling to G protein coupled receptors (GPCRs) is well characterized, the mechanisms underlying selective interactions between distinct Gα subtypes (Gαs, Gαi, Gαq, and Gα12/13) and Gβγ remain poorly understood. While conserved residues in Gα subtypes are often assumed to have similar functions, they may instead modulate coupling selectivity by altering the freq...

Topics

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• Allosteric Regulation
• Bayes Theorem
• GTP-Binding Protein alpha Subunits
• GTP-Binding Protein alpha Subunits, Gq-G11
• GTP-Binding Protein alpha Subunits, Gs
• Molecular Dynamics Simulation
• Mutation
• Receptors, G-Protein-Coupled

Identifiers and source

Literature Corpus work

1172eca1-74a5-579a-8ab0-b0b96d49d8e1

DOI

10.64898/2026.01.29.702674