BMS2021 Lecture Notes - Lecture 4: Lipophilicity, Inositol, Apoptosis
15 Aug 2018
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Transmembrane proteins with their ligand-binding domain on the outer surface of the plasma membrane. Instead of having a cytosolic domain that associates with a trimeric g-protein, it has an intrinsic enzyme activity or associates directly with an enzyme. Understand how receptor tyrosine kinases relay signals in the cell. Tyrosine-kinase-associated receptors: couple to separate proteins that have tyr kinase activity. Be able to distinguish the features of the rtk pathway. Many extracellular signal proteins (e. g. secreted and cell-surface-bound proteins that control cell behaviour) ~60 human rtks (classified into about 20 structural subfamilies each dedicated to its complementary family of protein ligands) In absence of the ligand, the egf receptor exists as an inactive monomer. Egf binding = conformational change that promotes dimerization of the external domains. Dimerization orients the internal kinase domains into an asymmetric dimer. O(cid:374)e ki(cid:374)ase do(cid:373)ai(cid:374) (cid:894)the (cid:862)a(cid:272)ti(cid:448)ator(cid:895) pushes agai(cid:374)st the other ki(cid:374)ase do(cid:373)ai(cid:374) (cid:894)the (cid:862)re(cid:272)ei(cid:448)er(cid:863)(cid:895) This causes an activating conformational change in the receive.
