1HCF
Crystal structure of TrkB-d5 bound to neurotrophin-4/5
Summary for 1HCF
Entry DOI | 10.2210/pdb1hcf/pdb |
Related | 1B8M 1B98 1WWB |
Descriptor | NEUROTROPHIN-4, BDNF/NT-3 GROWTH FACTORS RECEPTOR, SULFATE ION, ... (4 entities in total) |
Functional Keywords | transferase/hormone, complex(transferase-growth factor), neurotrophin-4/5, trkb receptor, ngf-beta superfamily, immunoglobulin domain, transferase-hormone complex |
Biological source | HOMO SAPIENS (HUMAN) More |
Cellular location | Secreted: P34130 Membrane; Single-pass type I membrane protein: Q16620 |
Total number of polymer chains | 4 |
Total formula weight | 51365.50 |
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 citation | Banfield, 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: 11738045DOI: 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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