AP BIOLOGY

Detailed explanation-1: -The dimerization brings the intracellular domains of two RTKs in proximity. As a result, the kinase domains on these intracellular domains can trans-phosphorylate each other on specific tyrosine amino acid residues.

Detailed explanation-2: -RTKs are characterised by the dimerisation of two receptor chains with an N-terminal (N) extracellular domain (ECM), and a C-terminal (C) intracellular domain (ICD). The extracellular domain is implicated in the recognition of the dimeric ligands and the formation of the receptor chain dimerisation process.

Detailed explanation-3: -These autoinhibitory interactions differ in detail among the TKDs, but in all cases they involve key tyrosines in the juxtamembrane region. Receptor dimerization promotes trans-phosphorylation of these tyrosines, which disrupts the cis-autoinhibitory interactions and promotes receptor activation (Hubbard, 2004).

Detailed explanation-4: -When signaling molecules bind to RTKs, they cause neighboring RTKs to associate with each other, forming cross-linked dimers. Cross-linking activates the tyrosine kinase activity in these RTKs through phosphorylation-specifically, each RTK in the dimer phosphorylates multiple tyrosines on the other RTK.

Detailed explanation-5: -3 Tyrosine Kinase Inhibitors Tyrosine phosphorylation of plasmalemmal receptors or other proteins provides high-affinity binding sites for src homology 2 (SH2)-containing proteins and represents a key targeting mechanism for enzyme translocation.