High affinity nerve growth factor receptor
FunctionHigh affinity nerve growth factor receptor (TrkA) is a tyrosine kinase receptor. Trk stands for Topomyosin-Related Kinase. TrkA ligand - nerve growth factor activates the receptor by stabilizing homodimer formation which initiates transautophosphorylation[1]. See also Neurotrophin. RelevanceTrkA has a role in the pathogenesis of psoriasis and its inhibitors are studied in the development of novel therapeutics for the disease[1]. TrkA inhibition may be a novel therapeutic approach to Alzheimer disease[2] and a new method to treat intractable pain[3]. Structural highlights. An , 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[4], [5]. .
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3D structures of high affinity nerve growth factor receptor3D structures of high affinity nerve growth factor receptor
Updated on 16-May-2023
ReferencesReferences
- ↑ 1.0 1.1 Gill JS, Windebank AJ. Direct activation of the high-affinity nerve growth factor receptor by a non-peptide symmetrical polyanion. Neuroscience. 1998 Dec;87(4):855-60. PMID:9759973
- ↑ Zhang Q, Descamps O, Hart MJ, Poksay KS, Spilman P, Kane DJ, Gorostiza O, John V, Bredesen DE. Paradoxical effect of TrkA inhibition in Alzheimer's disease models. J Alzheimers Dis. 2014;40(3):605-617. doi: 10.3233/JAD-130017. PMID:24531152 doi:http://dx.doi.org/10.3233/JAD-130017
- ↑ Hirose M, Kuroda Y, Murata E. NGF/TrkA Signaling as a Therapeutic Target for Pain. Pain Pract. 2016 Feb;16(2):175-82. doi: 10.1111/papr.12342. Epub 2015 Aug 27. PMID:26452158 doi:http://dx.doi.org/10.1111/papr.12342
- ↑ 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