High affinity nerve growth factor receptor
From Proteopedia
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== Structural highlights == | == 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<ref>PMID:17196528</ref>, <ref>PMID:10490030</ref>. | ||
</StructureSection> | </StructureSection> | ||
Revision as of 07:24, 27 December 2018
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3D structures of high affinity nerve growth factor receptor
Updated on 27-December-2018
References
- ↑ 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
- ↑ 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
- ↑ 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
