High-resolution cryo-electron microscopy structures of murine norovirus 1 and rabbit hemorrhagic disease virus reveal marked flexibility in the receptor binding domains

Journal of Virology

Volumn 84, Issue 11, 2010, Pages 5836-5841

  Katpally, Umesh ^a   Voss, Neil R ^b   Cavazza, Tommaso ^a   Taube, Stefan ^c   Rubin, John R ^e   Young, Vivienne L ^d   Stuckey, Jeanne ^e   Ward, Vernon K ^d   Virgin IV, Herbert W ^f   Wobus, Christiane E ^c   Smith, Thomas J ^a  

^a DONALD DANFORTH PLANT SCIENCE CENTER   (United States)

^b SCRIPPS RESEARCH INSTITUTE   (United States)

^c UNIVERSITY OF MICHIGAN MEDICAL SCHOOL   (United States)

^d UNIVERSITY OF OTAGO   (New Zealand)

^e UNIVERSITY OF MICHIGAN   (United States)

^f WASHINGTON UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CAPSID PROTEIN;

ARTICLE; CELL SURFACE; HIGH RESOLUTION CRYO ELECTRON MICROSCOPY; LAGOVIRUS; MURINE NOROVIRUS 1; NONHUMAN; NOROVIRUS; PRIORITY JOURNAL; PROTEIN DOMAIN; RECEPTOR BINDING; THREE DIMENSIONAL IMAGING; VIRION; VIRUS CELL INTERACTION; VIRUS LIKE AGENT; VIRUS MORPHOLOGY;

ANIMALS; BINDING SITES; CRYOELECTRON MICROSCOPY; HEMORRHAGIC DISEASE VIRUS, RABBIT; IMAGING, THREE-DIMENSIONAL; MICE; NOROVIRUS; PLIABILITY; PROTEIN CONFORMATION; RABBITS; RECEPTORS, VIRUS;

MURINE NOROVIRUS 1; RABBIT HEMORRHAGIC DISEASE VIRUS;

EID: 77951983848     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.00314-10     Document Type: Article

References (15)

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