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1HCF

Crystal structure of TrkB-d5 bound to neurotrophin-4/5

Summary for 1HCF
Entry DOI10.2210/pdb1hcf/pdb
Related1B8M 1B98 1WWB
DescriptorNEUROTROPHIN-4, BDNF/NT-3 GROWTH FACTORS RECEPTOR, SULFATE ION, ... (4 entities in total)
Functional Keywordstransferase/hormone, complex(transferase-growth factor), neurotrophin-4/5, trkb receptor, ngf-beta superfamily, immunoglobulin domain, transferase-hormone complex
Biological sourceHOMO SAPIENS (HUMAN)
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Cellular locationSecreted: P34130
Membrane; Single-pass type I membrane protein: Q16620
Total number of polymer chains4
Total formula weight51365.50
Authors
Banfield, M.J.,Naylor, R.L.,Robertson, A.G.S.,Allen, S.J.,Dawbarn, D.,Brady, R.L. (deposition date: 2001-05-03, release date: 2001-12-06, Last modification date: 2023-12-13)
Primary citationBanfield, M.J.,Naylor, R.L.,Robertson, A.G.S.,Allen, S.J.,Dawbarn, D.,Brady, R.L.
Specificity in Trk-Receptor:Neurotrophin Interaction: The Crystal Structure of Trkb-D5 in Complex with Neurotrophin-4/5
Structure, 9:1191-, 2001
Cited by
PubMed Abstract: The binding of neurotrophin ligands to their respective Trk cellular receptors initiates intracellular signals essential for the growth and survival of neurons. The site of neurotrophin binding has been located to the fifth extracellular domain of the Trk receptor, with this region regulating both the affinity and specificity of Trk receptor:neurotrophin interaction. Neurotrophin function has been implicated in a number of neurological disorders, including Alzheimer's disease and Parkinson's disease.
PubMed: 11738045
DOI: 10.1016/S0969-2126(01)00681-5
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.7 Å)
Structure validation

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