p10191-10193, 10195,11600 to FAH
Posted: Thu Dec 03, 2015 7:06 pm
For this project, we are studying the switching of Gq proteins between "inactive" state and "active" state:
The heterotrimeric Gq proteins are molecular switches that perceive the signal from G-protein-coupled receptors (GPCRs) to regulate the physiological behaviors of its downstream protein-beta isoform of phospholipase C (beta-PLC). This pivotal role makes Gq proteins essential players in cardiac physiology and pathophysiology. To perform its key functions in regulating the beta-PLC, the heterotrimeric Gq proteins need to switch between "active" and "inactive" states. In the “active” state, the Gq protein binds to a GTP molecule to regulate the activation of beta-PLC, and in the "inactive" state, the Gq protein binds to a GDP molecule and can be recruited by GPCRs, which catalyze the exchange of the GDP to a GTP. The molecular mechanism underpinning the switching between the "inactive" state and the "active" state is still unclear. The objective of this project is to understand this switching. The results from this work would greatly advance our understanding of the pivoted roles that Gq proteins play and facilitate drug discovery targeting Gq.
http://fah-web.stanford.edu/cgi-bin/fah ... ed?p=10191
Project Leader: Greg Bowman and Xianqiang (Leos) Sun. Washington University in St. Louis
Atoms: 62300
Credit: 1273
Timeout: 6 days
Deadline: 20 days
The heterotrimeric Gq proteins are molecular switches that perceive the signal from G-protein-coupled receptors (GPCRs) to regulate the physiological behaviors of its downstream protein-beta isoform of phospholipase C (beta-PLC). This pivotal role makes Gq proteins essential players in cardiac physiology and pathophysiology. To perform its key functions in regulating the beta-PLC, the heterotrimeric Gq proteins need to switch between "active" and "inactive" states. In the “active” state, the Gq protein binds to a GTP molecule to regulate the activation of beta-PLC, and in the "inactive" state, the Gq protein binds to a GDP molecule and can be recruited by GPCRs, which catalyze the exchange of the GDP to a GTP. The molecular mechanism underpinning the switching between the "inactive" state and the "active" state is still unclear. The objective of this project is to understand this switching. The results from this work would greatly advance our understanding of the pivoted roles that Gq proteins play and facilitate drug discovery targeting Gq.
http://fah-web.stanford.edu/cgi-bin/fah ... ed?p=10191
Project Leader: Greg Bowman and Xianqiang (Leos) Sun. Washington University in St. Louis
Atoms: 62300
Credit: 1273
Timeout: 6 days
Deadline: 20 days