4qv2
Unliganded crystal structure of Feline Norovirus P Domain co-crystallized with HBGA A-trisaccharideUnliganded crystal structure of Feline Norovirus P Domain co-crystallized with HBGA A-trisaccharide
Structural highlights
Publication Abstract from PubMedNorovirus infects different animals, including humans, mice, dogs, and cats. Here, we show an X-ray crystal structure of a feline GIV.2 norovirus capsid-protruding (P) domain to 2.35A resolution. The feline GIV.2 P domain was reminiscent of human norovirus P domains, except for a novel P2 subdomain alpha-helix and an extended P1 subdomain interface loop. These new structural features likely obstructed histo-blood group antigens, which are attachment factors for human norovirus, from binding at the equivalent sites on the feline GIV.2 P domain. Additionally, an ELISA showed that the feline GIV.2 was antigenically distinct from a human GII.10 norovirus. Structural analysis of a feline norovirus protruding domain.,Singh BK, Glatt S, Ferrer JL, Koromyslova AD, Leuthold MM, Dunder J, Hansman GS Virology. 2015 Jan 1;474:181-5. doi: 10.1016/j.virol.2014.10.028. Epub 2014 Nov, 19. PMID:25463616[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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