6OAS
Structure of canine parvovirus in complex with transferrin receptor type-1
Summary for 6OAS
| Entry DOI | 10.2210/pdb6oas/pdb |
| EMDB information | 20001 20002 20003 |
| Descriptor | Capsid protein VP1 (1 entity in total) |
| Functional Keywords | cpv, tfr, icosahedral, cryo, virus |
| Biological source | Canine parvovirus 2 (CPV-2) |
| Total number of polymer chains | 1 |
| Total formula weight | 61562.37 |
| Authors | Lee, H.,Hafenstein, S. (deposition date: 2019-03-18, release date: 2019-09-18, Last modification date: 2024-11-06) |
| Primary citation | Lee, H.,Callaway, H.M.,Cifuente, J.O.,Bator, C.M.,Parrish, C.R.,Hafenstein, S.L. Transferrin receptor binds virus capsid with dynamic motion. Proc.Natl.Acad.Sci.USA, 116:20462-20471, 2019 Cited by PubMed Abstract: Canine parvovirus (CPV) is an important pathogen causing severe diseases in dogs, including acute hemorrhagic enteritis, myocarditis, and cerebellar disease. Cross-species transmission of CPV occurs as a result of mutations on the viral capsid surface that alter the species-specific binding to the host receptor, transferrin receptor type-1 (TfR). The interaction between CPV and TfR has been extensively studied, and previous analyses have suggested that the CPV-TfR complex is asymmetric. To enhance the understanding of the underlying molecular mechanisms, we determined the CPV-TfR interaction using cryo-electron microscopy to solve the icosahedral (3.0-Å resolution) and asymmetric (5.0-Å resolution) complex structures. Structural analyses revealed conformational variations of the TfR molecules relative to the binding site, which translated into dynamic molecular interactions between CPV and TfR. The precise footprint of the receptor on the virus capsid was identified, along with the identity of the amino acid residues in the virus-receptor interface. Our "rock-and-roll" model provides an explanation for previous findings and gives insights into species jumping and the variation in host ranges associated with new pandemics in dogs. PubMed: 31548398DOI: 10.1073/pnas.1904918116 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3 Å) |
Structure validation
Download full validation report
