[HTML][HTML] RGK small GTP-binding proteins interact with the nucleotide kinase domain of Ca2+-channel β-subunits via an uncommon effector binding domain
P Béguin, YJA Ng, C Krause, RN Mahalakshmi… - Journal of biological …, 2007 - ASBMB
RGK proteins (Kir/Gem, Rad, Rem, and Rem2) form a small subfamily of the Ras
superfamily. Despite a conserved GTP binding core domain, several differences suggest
that structure, mechanism of action, and functional regulation differ from Ras. RGK proteins
down-regulate voltage-gated calcium channel activity by binding in a GTP-dependent
fashion to the Ca v β subunits. Mutational analysis combined with homology modeling
reveal a novel effector binding mechanism distinct from that of other Ras GTPases. In this …
superfamily. Despite a conserved GTP binding core domain, several differences suggest
that structure, mechanism of action, and functional regulation differ from Ras. RGK proteins
down-regulate voltage-gated calcium channel activity by binding in a GTP-dependent
fashion to the Ca v β subunits. Mutational analysis combined with homology modeling
reveal a novel effector binding mechanism distinct from that of other Ras GTPases. In this …