PLC beta 3 Gq: Difference between revisions

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PLC-β3 interacts with a surface on Gαq that <scene name='70/701452/Fig5/1'>overlaps almost completely</scene> with portions of Gα subunits needed for engagement of RGS proteins and the effector-binding region. Other effectors are known to engage the <scene name='70/701452/Fig3/1'>effector-binding site</scene> within Gα subunits. There are a large family of regulator of G protein signaling (RGS) proteins that independently accelerates the GTP hydrolysis in the <scene name='70/701452/Fig4/1'>GTPase domain</scene>.
PLC-β3 interacts with a surface on Gαq that <scene name='70/701452/Fig5/1'>overlaps almost completely</scene> with portions of Gα subunits needed for engagement of RGS proteins and the effector-binding region. Other effectors are known to engage the <scene name='70/701452/Fig3/1'>effector-binding site</scene> within Gα subunits. There are a large family of regulator of G protein signaling (RGS) proteins that independently accelerates the GTP hydrolysis in the <scene name='70/701452/Fig4/1'>GTPase domain</scene>.


The canonical Gα effector-binding region of Gαq, located between α3 and switch 2, is occupied by a helix-turn-helix (Hα1/Hα2) that immediately follows the C2 domain of PLC- β3. <scene name='70/701452/Pro862/1'>Pro862</scene> of PLC- β3 lies within the turn between Hα1 and Hα2, makes extensive contacts with multiple residues of Gαq, and forms the center of a Gαq-binding interface.
The canonical Gα effector-binding region of Gαq, located between α3 and switch 2, is occupied by a helix-turn-helix (Hα1/Hα2) that immediately follows the C2 domain of PLC- β3. <scene name='70/701452/Pro862/2'>TextToBeDisplayed</scene> of PLC- β3 lies within the turn between Hα1 and Hα2, makes extensive contacts with multiple residues of Gαq, and forms the center of a Gαq-binding interface.


<scene name='70/701452/Fig6/3'>The loop</scene> between the end of the TIM barrel and the beginning of the C2 domain comprises a second distinct segment of PLC- β3 that makes extensive contacts with active Gαq, including switches 1 and 2. This interface includes a series of interdigitated pairs of charged residues, specifically in PLC- β3-Gαq Asp709/Arg202, Lys710/Glu191, and Asp721/Lys41; these in turn are supported by additional charged residues Glu703 and Arg707 of PLC- β3.
<scene name='70/701452/Fig6/3'>The loop</scene> between the end of the TIM barrel and the beginning of the C2 domain comprises a second distinct segment of PLC- β3 that makes extensive contacts with active Gαq, including switches 1 and 2. This interface includes a series of interdigitated pairs of charged residues, specifically in PLC- β3-Gαq Asp709/Arg202, Lys710/Glu191, and Asp721/Lys41; these in turn are supported by additional charged residues Glu703 and Arg707 of PLC- β3.

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Shir Navot, Michal Harel, Joel L. Sussman