Biology 2382B Lecture Notes - Lecture 9: Erbb4, Gtpase, Epitope

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A-h. = simple coil of amino acids. Intrinsic tyrosine kinase activity which is activated by ligand binding and receptor dimerization. Will bind to receptor at the activated phosphate and will pass signal along to another molecule. Often this molecule is an enzyme of some sort, ras for. Ras acts as a gtpase switch protein to signal further downstream" example kinases. Aberrant signaling is at the root of many human cancers - because they trigger lots of changes in the cell cycle genes. Protein tyrosine kinase does nothing (inactive) without bound ligand. Conformational change in receptors (2); which facilitate dimerization. Dimerization allows for trans-autophosphorylation of cytoplasmic domains (enzyme domain) Trans-autophosphorylation = acts itself to put phosphates on tyrosine; but one half of the dimer (one receptor) phosphorylates the other side of the dimer (other receptor) Lip-tyrosines are phosphorylated initially - they act as a starting point for the rest of the tyrosines on the rtk.

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