Structural homology discloses a bifunctional structural motif at the N-termini of G(sub)alpha proteins

Results from homology modeling reveal that the heterotrimeric human G(sub)alpha proteins exhibit a basic, positively charged, structural motif at the N-termini, which influence both membrane affinity and orientation of the G proteins. Data further suggest that the alpha-helical basic motif participates in the membrane-targeting and palmitylation-determining signaling.