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| == Function == | | == Function == |
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| '''High affinity nerve growth factor receptor''' (TrkA) is a tyrosine kinase receptor. TrkA ligand - nerve growth factor activates the receptor by stabilizing homodimer formation which initiates transautophosphorylation<ref>PMID:9759973</ref>. | | '''High affinity nerve growth factor receptor''' (TrkA) is a tyrosine kinase receptor. TrkA ligand - nerve growth factor activates the receptor by stabilizing homodimer formation which initiates transautophosphorylation<ref> name="TrkA">PMID:9759973</ref>. |
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| == Disease == | | == Disease == |
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| == Relevance == | | == Relevance == |
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| TrkA has a role in the pathogenesis of psoriasis and its inhibitors are studied in the development of novel therapeutics for the disease<ref>PMID:9759973</ref>. | | TrkA has a role in the pathogenesis of psoriasis and its inhibitors are studied in the development of novel therapeutics for the disease<ref name="TrkA"/>. |
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| == Structural highlights == | | == Structural highlights == |
Revision as of 07:27, 27 December 2018
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Function
High affinity nerve growth factor receptor (TrkA) is a tyrosine kinase receptor. TrkA ligand - nerve growth factor activates the receptor by stabilizing homodimer formation which initiates transautophosphorylation[1].
Disease
Relevance
TrkA has a role in the pathogenesis of psoriasis and its inhibitors are studied in the development of novel therapeutics for the disease[2].
Structural highlights
An Arg residue, conserved in all neutrophins, forms the most important binding determinant between TrkA and its ligand - nerve growth factor - which forms the active homodimer of the receptor[3], [4].
- ↑ name="TrkA">PMID:9759973
- ↑ Cite error: Invalid
<ref> tag; no text was provided for refs named TrkA
- ↑ 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
- ↑ Wiesmann C, Ultsch MH, Bass SH, de Vos AM. Crystal structure of nerve growth factor in complex with the ligand-binding domain of the TrkA receptor. Nature. 1999 Sep 9;401(6749):184-8. PMID:10490030 doi:10.1038/43705
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3D structures of high affinity nerve growth factor receptor
Updated on 27-December-2018
{"openlevels":0}
- High affinity nerve growth factor receptor; Domains – nerve growth factor-binding 36-383; transmembrane 410-447; catalytic+juxtamembrane 376-698; kinase 498-796
- 1he7 – hTrkA residues 282-413 – human
- 2n90 – hTrkA transmembrane domain – NMR
- 4crp – hTrkA nerve growth factor-binding domain (mutant) – NMR
- 4f0i, 4gt5 – hTrkA kinase domain
- High affinity nerve growth factor receptor complex
- 5kvt, 5wr7 – hTrkA kinase domain + anticancer drug
- 4aoj, 4pmm, 4pmp, 4pms, 4pmt, 4yne, 4yps, 5h3q, 6dkb, 6dkg, 6dki, 6dkw – hTrkAChoE kinase domain + inhibitor
- 5kmj, 5kmk, 5kml, 5kmm, 5kmn, 5kmo, 6d1y, 6d1z, 6d20, 5i8a, 5jfs, 5jfv, 5jfw, 5jfx, 5kmi, – hTrkAChoE catalytic+juxtamembrane domains 376-698 + inhibitor
- 2ifg – hTrkAChoE nerve growth factor-binding domain + nerve growth factor
References
