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3TS3

Crystal structure of the projection domain of the turkey astrovirus capsid protein at 1.5 angstrom resolution

Summary for 3TS3
Entry DOI10.2210/pdb3ts3/pdb
DescriptorCapsid polyprotein, SULFATE ION (3 entities in total)
Functional Keywordsvirus protein, projection domain, astrovirus capsid, viral protein
Biological sourceTurkey astrovirus 2 (TAstV-2)
Cellular locationVirion (Potential): Q9Q3G5
Total number of polymer chains4
Total formula weight95650.75
Authors
DuBois, R.M.,Schultz-Cherry, S.,White, S.W. (deposition date: 2011-09-12, release date: 2011-09-28, Last modification date: 2024-02-28)
Primary citationDuBois, R.M.,Freiden, P.,Marvin, S.,Reddivari, M.,Heath, R.J.,White, S.W.,Schultz-Cherry, S.
Crystal structure of the avian astrovirus capsid spike.
J.Virol., 87:7853-7863, 2013
Cited by
PubMed Abstract: Astroviruses are small, nonenveloped, single-stranded RNA viruses that cause diarrhea in a wide variety of mammals and birds. On the surface of the viral capsid are globular spikes that are thought to be involved in attachment to host cells. To understand the basis of species specificity, we investigated the structure of an avian astrovirus capsid spike and compared it to a previously reported human astrovirus capsid spike structure. Here we report the crystal structure of the turkey astrovirus 2 (TAstV-2) capsid surface spike domain, determined to 1.5-Å resolution, and identify three conserved patches on the surface of the spike that are candidate avian receptor-binding sites. Surprisingly, the overall TAstV-2 capsid spike structure is unique, with only distant structural similarities to the human astrovirus capsid spike and other viral capsid spikes. There is an absence of conserved putative receptor-binding sites between the human and avian spikes. However, there is evidence for carbohydrate-binding sites in both human and avian spikes, and studies with human astrovirus 1 (HAstV-1) suggest a minor role in infection for chondroitin sulfate but not heparin. Overall, our structural and functional studies provide new insights into astrovirus host cell entry, species specificity, and evolution.
PubMed: 23658448
DOI: 10.1128/JVI.03139-12
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.49 Å)
Structure validation

226707

数据于2024-10-30公开中

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