BIO230H1 Lecture Notes - Lecture 9: Ras Superfamily, Small Gtpase, Gtpase
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BIO230H1 Full Course Notes
Verified Note
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Document Summary
Enzyme coupled receptors are transmembrane proteins with ligand- binding domain. Many extracellular signals can be determined by receptor tyrosine kinases. Phosphorylated tyrosine on rtks serve as docking sites for intracellular. Cross phosphorylation can occur; first phosphorylating the kinase domain then the kinase domain creates a docking site. Proteins with sh2 domains binds to phosphorylated tyrosine. Ras belongs to a large superfamily of monomeric gtpase. Ras can cycle between gtp and gdp. Rtks activate via adaptors and gefs evidence from the developing drosophila. Bride of sevenless (boss): encodes for a ligand. Ras can help activate activity through phosphorylation. Scaffold molecules help line up the molecules. Receptor serine/threonine kinases are the large class of cell surface. Lv3 intercats with clv2 and clv1 to provide transcriptional sequences. Serine/threonine and tyrosine protein kinases are structurally related. The complexes are structurally related to one another. Bacterial chemotaxis depends on a two component signaling pathway. The receptor protein notch is a latent gene regulatory proteins.
