PLC beta 3 Gq: Difference between revisions

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PLC- β3 engages Gαq throughout three regions. First, an extended loop between the third and fourth EF hands of PLC- β3 directly buttresses switch residues critical for GTP hydrolysis by Gαq. Second, the region of PLC- β3 that connects the catalytic TIM barrel and the C2 domain interacts with both switches 1 and 2 of Gαq. Third, a segment composed of a helix-turn-helix at the C terminus of the C2 domain resides primarily within a shallow declivity on the surface of Gαq formed by switch 2 and α3.
PLC- β3 engages Gαq throughout three regions. First, an extended loop between the third and fourth EF hands of PLC- β3 directly buttresses switch residues critical for GTP hydrolysis by Gαq. Second, the region of PLC- β3 that connects the catalytic TIM barrel and the C2 domain interacts with both switches 1 and 2 of Gαq. Third, a segment composed of a helix-turn-helix at the C terminus of the C2 domain resides primarily within a shallow declivity on the surface of Gαq formed by switch 2 and α3.


Other effectors are known to engage the effector-binding site within Gα subunits. There are a large family of regulator of G protein signaling (RGS) proteins that independently accelerate the GTP hydrolysis in the GTPase domain. PLC-β3 interacts with a surface on Gαq that overlaps almost completely with portions of Gα subunits needed for engagement of RGS proteins and the effector-binding region.
PLC-β3 interacts with a surface on Gαq that overlaps almost completely with portions of Gα subunits needed for engagement of RGS proteins and the effector-binding region. Other effectors are known to engage the effector-binding site within Gα subunits. There are a large family of regulator of G protein signaling (RGS) proteins that independently accelerate the GTP hydrolysis in the GTPase domain.
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Shir Navot, Michal Harel, Joel L. Sussman