Receptor tyrosine kinases: Difference between revisions
Jump to navigation
Jump to search
m Created the page Receptor Tyrosine Kinases, Created a link to Enzyme coupled receptors (and referenced) |
m Added some more detail to the page I created about grb2 proteins in the Res pathway and added a link to guanine nucleotide exchange factor |
||
Line 1: | Line 1: | ||
Receptor tyrosine kinases are a common type of [[Enzyme-coupled Receptor|Enzyme Coupled receptors]] <ref>Alberts.B, Johnson.A, Lewis.J , Morgan.D , Raff.M ,Roberts.K , Walter.P Molecular Biology of the Cell 6th edition Garland Science</ref>.Receptor tyrosine kinases have a cystolic domain with intrinsic kinase activity. The binding of extracellular ligands trigger cross phosphorylation of the tyrosine kinase domain. Proteins are then able to bind to the phosphorylated tyrosines.<references /> | Receptor tyrosine kinases are a common type of [[Enzyme-coupled Receptor|Enzyme Coupled receptors]] <ref>Alberts.B, Johnson.A, Lewis.J , Morgan.D , Raff.M ,Roberts.K , Walter.P Molecular Biology of the Cell 6th edition Garland Science</ref>.Receptor tyrosine kinases have a cystolic domain with intrinsic kinase activity. The binding of extracellular ligands trigger cross phosphorylation of the tyrosine kinase domain. Proteins are then able to bind to the phosphorylated tyrosines. Proteins such as Grb2 adaptor protein (involved in the [[Ras pathway|Ras pathway]]) which has the ability to bind to one of the phosphate groups on specific tyrosine residues. This, consequentially, recruits a [[Guanine nucleotide exchange factor|Guanine nucleotide exchange factor]] that activate monomeric GTPases by stimulating release of GDP to allow binding of GTP. <references /> |
Revision as of 19:24, 4 December 2016
Receptor tyrosine kinases are a common type of Enzyme Coupled receptors [1].Receptor tyrosine kinases have a cystolic domain with intrinsic kinase activity. The binding of extracellular ligands trigger cross phosphorylation of the tyrosine kinase domain. Proteins are then able to bind to the phosphorylated tyrosines. Proteins such as Grb2 adaptor protein (involved in the Ras pathway) which has the ability to bind to one of the phosphate groups on specific tyrosine residues. This, consequentially, recruits a Guanine nucleotide exchange factor that activate monomeric GTPases by stimulating release of GDP to allow binding of GTP.
- ↑ Alberts.B, Johnson.A, Lewis.J , Morgan.D , Raff.M ,Roberts.K , Walter.P Molecular Biology of the Cell 6th edition Garland Science