RESEARCH: G-PROTEINS
FOLDING PROJECT #17222 PROFILE

G-proteins are essential for many bodily functions like sight and smell. They switch between active and inactive states based on molecules called GDP and GTP. The project relates to understanding how G-proteins release GDP, a crucial step in activation, as problems with this process can cause diseases.

G-proteins play central role in various signalling pathways involved in vision, taste, oflaction, muscle contraction and neurotransmission.

G-proteins regulate these signalling pathways by switching between 'active' and 'inactive' states, dictated by the type nucleotide bound to their active site.

When bound to gaunosine dinucleotide (GDP), G-proteins adopt inactive state.

Dissociation of GDP and subsequent binding of gaunosine trinucleotide (GTP) activates G-proteins, which in turn activate downstream signalling pathways.

GDP dissociation is the rate limiting step in activation of G-proteins and misregulation of this process can often lead to disease conditions.

in this project, we are studying the mechanism of GDP dissociation process.

G-proteins

Guanine nucleotide-binding proteins involved in signal transduction.

G-proteins are crucial for transmitting signals within cells. They act like molecular switches, turning on and off various cellular processes like vision, taste, muscle contraction, and nerve impulses. This switching is controlled by binding to different molecules called GDP and GTP.

GDP

Guanosine Diphosphate

GDP is a molecule that G-proteins bind to in their inactive state. It helps keep the protein switched off until it needs to transmit a signal.

GTP

Guanosine Triphosphate

GTP is a molecule that activates G-proteins. When a G-protein binds to GTP, it switches into an active state and can start transmitting signals.