Biochemistry 3381A Study Guide - Quiz Guide: Conformational Change, Gtpase, Molecular Switch
Document Summary
Enzyme-coupled receptors are transmembrane proteins with the ligand binding domain on the outer surface of the membrane and a cytosolic domain which has either intrinsic enzyme activity or associates directly with an enzyme. Rtks consist in an inactive state as 2 monomers in which the internal kinase domain is inactive. Binding of signal on the extracellular domain of the receptor. Signal can be a dimer or monomer which simultaneously bind to the rtks and causes the receptors to dimerize thereby bringing the 2 cytoplasmic kinase domains together and thereby promoting their activation (conformational change) In most cases this enables the 2 kinase domains to phosphorylate each other which can have 2 effects: Phosphorylation at some tyrosines in the kinase domains promotes the complete activation of the domains. Phosphorylation at some tyrosines in other parts of the receptor generates docking sites for intracellular signalling proteins, resulting in the formation of large signalling complexes that can broadcast signals among multiple signalling pathways.