2NSU
Crystal structure of the ectodomain of human transferrin receptor fitted into a cryo-EM reconstruction of canine parvovirus and feline transferrin receptor complex
Summary for 2NSU
| Entry DOI | 10.2210/pdb2nsu/pdb |
| Related | 1CX8 |
| EMDB information | 1288 |
| Descriptor | Transferrin receptor protein 1 (1 entity in total) |
| Functional Keywords | transferrin receptor, virus-receptor complex, metal transport |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 2 |
| Total formula weight | 143245.92 |
| Authors | Hafenstein, S.,Kostyuchenko, V.A.,Rossmann, M.G. (deposition date: 2006-11-06, release date: 2007-03-27, Last modification date: 2024-11-13) |
| Primary citation | Hafenstein, S.,Palermo, L.M.,Kostyuchenko, V.A.,Xiao, C.,Morais, M.C.,Nelson, C.D.,Bowman, V.D.,Battisti, A.J.,Chipman, P.R.,Parrish, C.R.,Rossmann, M.G. Asymmetric binding of transferrin receptor to parvovirus capsids. Proc.Natl.Acad.Sci.Usa, 104:6585-6589, 2007 Cited by PubMed Abstract: Although many viruses are icosahedral when they initially bind to one or more receptor molecules on the cell surface, such an interaction is asymmetric, probably causing a breakdown in the symmetry and conformation of the original infecting virion in preparation for membrane penetration and release of the viral genome. Cryoelectron microscopy and biochemical analyses show that transferrin receptor, the cellular receptor for canine parvovirus, can bind to only one or a few of the 60 icosahedrally equivalent sites on the virion, indicating that either canine parvovirus has inherent asymmetry or binding of receptor induces asymmetry. The asymmetry of receptor binding to canine parvovirus is reminiscent of the special portal in tailed bacteriophages and some large, icosahedral viruses. Asymmetric interactions of icosahedral viruses with their hosts might be a more common phenomenon than previously thought and may have been obscured by averaging in previous crystallographic and electron microscopic structure determinations. PubMed: 17420467DOI: 10.1073/pnas.0701574104 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (27 Å) |
Structure validation
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