1S58
The structure of B19 parvovirus capsid
Summary for 1S58
| Entry DOI | 10.2210/pdb1s58/pdb |
| Related | 1FPV 1K3V 1LP3 1dnv 1mvm 4dpv |
| Descriptor | B19 parvovirus capsid (1 entity in total) |
| Functional Keywords | icosahedral capsid, beta-barrel, icosahedral virus, virus |
| Biological source | Human parvovirus B19 |
| Total number of polymer chains | 1 |
| Total formula weight | 60930.05 |
| Authors | Kaufmann, B.,Simpson, A.A.,Rossmann, M.G. (deposition date: 2004-01-20, release date: 2004-08-17, Last modification date: 2024-04-03) |
| Primary citation | Kaufmann, B.,Simpson, A.A.,Rossmann, M.G. The structure of human parvovirus B19. Proc.Natl.Acad.Sci.USA, 101:11628-11633, 2004 Cited by PubMed Abstract: Human parvovirus B19 is the only parvovirus known to be a human pathogen. The structure of recombinant B19-like particles has been determined to approximately 3.5-A resolution by x-ray crystallography and, to our knowledge, represents the first near-atomic structure of an Erythrovirus. The polypeptide fold of the major capsid protein VP2 is a "jelly roll" with a beta-barrel motif similar to that found in many icosahedral viruses. The large loops connecting the strands of the beta-barrel form surface features that differentiate B19 from other parvoviruses. Although B19 VP2 has only 26% sequence identity to VP3 of adeno-associated virus, 72% of the C(alpha) atoms can be aligned structurally with a rms deviation of 1.8 A. Both viruses require an integrin as a coreceptor, and conserved surface features suggest a common receptor-binding region. PubMed: 15289612DOI: 10.1073/pnas.0402992101 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.5 Å) |
Structure validation
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