3QSQ
Crystal structure of the projection domain of the human astrovirus capsid protein
Summary for 3QSQ
| Entry DOI | 10.2210/pdb3qsq/pdb |
| Descriptor | Capsid polyprotein (2 entities in total) |
| Functional Keywords | receptor binding domain, astrovirus capsid, viral protein |
| Biological source | Human astrovirus 8 (HAstV-8) |
| Cellular location | Virion (Potential): Q9IFX1 |
| Total number of polymer chains | 1 |
| Total formula weight | 27222.50 |
| Authors | Dong, J.,Dong, L.,Mendez, E.,Tao, Y.J. (deposition date: 2011-02-21, release date: 2011-07-20, Last modification date: 2024-02-21) |
| Primary citation | Dong, J.,Dong, L.,Mendez, E.,Tao, Y. Crystal structure of the human astrovirus capsid spike. Proc.Natl.Acad.Sci.USA, 108:12681-12686, 2011 Cited by PubMed Abstract: Astroviruses are single-stranded, plus-sense RNA viruses that infect both mammals and birds, causing gastroenteritis and other extraintestinal diseases. Clinical studies have established astroviruses as the second leading cause of viral diarrhea in young children. Here we report the crystal structure of the human astrovirus dimeric surface spike determined to 1.8-Å resolution. The overall structure of each spike/projection domain has a unique three-layered β-sandwiches fold, with a core, six-stranded β-barrel structure that is also found in the hepatitis E virus capsid protrusions, suggesting a closer phylogenetic relationship between these two viruses than previously acknowledged. Based on a hepatitis E virus capsid model, we performed homology modeling and produced a complete, T = 3 astrovirus capsid model with features remarkably similar to those observed in a cryoelectron microscopy reconstruction image of a human astrovirus. Mapping conserved residues onto the astrovirus projection domain revealed a putative receptor binding site with amino acid compositions characteristic for polysaccharide recognition. Our results will have an important impact on future characterization of astrovirus structure and function, and will likely have practical applications in the development of vaccines and antivirals. PubMed: 21768348DOI: 10.1073/pnas.1104834108 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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