Tyrosine kinase receptor

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== Function ==
== Function ==
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'''Tyrosine kinase receptor''' or '''high affinity nerve growth factor receptor''' (TRK-A) play an important role in cellular processes like growth, motility, differentiation and metabolism<ref>PMID:29455648</ref>. Nerve growth factor (NGF) is a neutrotrophin which binds with high affinity to TRK. The binding of NGF to TRK-A activates the latter which undergoes dimerization and autophosphorylation at several Tyr residues that selectively trigger activity in several intercellular signaling pathways via binding of specific effector proteins<ref>PMID:24668471</ref>.
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'''Tyrosine kinase receptor''' or '''high affinity nerve growth factor receptor''' (TRK-A) play an important role in cellular processes like growth, motility, differentiation and metabolism<ref>PMID:29455648</ref>. Nerve growth factor (NGF) is a neutrotrophin which binds with high affinity to TRK. The binding of NGF to TRK-A activates the latter which undergoes dimerization and autophosphorylation at several Tyr residues that selectively trigger activity in several intercellular signaling pathways via binding of specific effector proteins<ref>PMID:24668471</ref>. See also [[High affinity nerve growth factor receptor]].
== Disease ==
== Disease ==

Revision as of 09:30, 31 March 2020

Human TRK-A kinase domain complex with inhibitor, MPD and sulfate (PDB code 6p11)

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3D Structures tyrosine kinase receptor

Updated on 31-March-2020

  • Tyrosine kinase receptor or high affinity nerve growth factor receptor; Domains – extracellular 36-382; LBD 285-380; transmembrane 410-447; kinase 498-796

1he7 – hTRK-A LBD domain – human
4crp – hTRK-A LBD domain (mutant) – NMR
2ifg – hTRK-A extracellular domain + b-nerve growth factor
4gt5, 4f0i] – hTRK-A kinase domain
5kvt, 6pl1, 6npt, 6nsp, 6nss, 5wr7, 6d1y, 6d1z, 6pmc, 6iqn, 6pl2, 6pl3, 6pma, 6pmb, 6pme, 5kmj, 5kmk, 5kmm, 5kmn, 5kmo, 4aoj, 4pmm, 4pmp, 4pms, 4pmt, 4yps, 5h3q, 5i8a, 5kmi, 5kml, 6d20, 6dkb, 6dkg, 6dki, 6j5l, 5jfs, 5jfv, 5jfw, 5jfx, 4yne, 6dkw – hTRK-A kinase domain + inhibitor
2n90 – hTRK-A transmembrane domain - NMR

References

  1. ↑ Du Z, Lovly CM. Mechanisms of receptor tyrosine kinase activation in cancer. Mol Cancer. 2018 Feb 19;17(1):58. doi: 10.1186/s12943-018-0782-4. PMID:29455648 doi:http://dx.doi.org/10.1186/s12943-018-0782-4
  2. ↑ Deinhardt K, Chao MV. Trk receptors. Handb Exp Pharmacol. 2014;220:103-19. doi: 10.1007/978-3-642-45106-5_5. PMID:24668471 doi:http://dx.doi.org/10.1007/978-3-642-45106-5_5
  3. ↑ Cassol CA, Winer D, Liu W, Guo M, Ezzat S, Asa SL. Tyrosine kinase receptors as molecular targets in pheochromocytomas and paragangliomas. Mod Pathol. 2014 Aug;27(8):1050-62. doi: 10.1038/modpathol.2013.233. Epub 2014, Jan 3. PMID:24390213 doi:http://dx.doi.org/10.1038/modpathol.2013.233
  4. ↑ Choi HS, Rucker PV, Wang Z, Fan Y, Albaugh P, Chopiuk G, Gessier F, Sun F, Adrian F, Liu G, Hood T, Li N, Jia Y, Che J, McCormack S, Li A, Li J, Steffy A, Culazzo A, Tompkins C, Phung V, Kreusch A, Lu M, Hu B, Chaudhary A, Prashad M, Tuntland T, Liu B, Harris J, Seidel HM, Loren J, Molteni V. (R)-2-Phenylpyrrolidine Substituted Imidazopyridazines: A New Class of Potent and Selective Pan-TRK Inhibitors. ACS Med Chem Lett. 2015 Mar 16;6(5):562-7. doi: 10.1021/acsmedchemlett.5b00050., eCollection 2015 May 14. PMID:26005534 doi:http://dx.doi.org/10.1021/acsmedchemlett.5b00050
  5. ↑ Wehrman T, He X, Raab B, Dukipatti A, Blau H, Garcia KC. Structural and mechanistic insights into nerve growth factor interactions with the TrkA and p75 receptors. Neuron. 2007 Jan 4;53(1):25-38. PMID:17196528 doi:10.1016/j.neuron.2006.09.034

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