Influenza viral hemagglutinin complicated shape is advantageous to its binding affinity for sialosaccharide receptor

Biochemical and Biophysical Research Communications

Volumn 355, Issue 1, 2007, Pages 6-9

  Sawada, Toshihiko ^a,c   Hashimoto, Tomohiro ^a   Nakano, Hirofumi ^b   Suzuki, Tohru ^a   Suzuki, Yasuo ^c,d   Kawaoka, Yoshihiro ^c,e,f   Ishida, Hideharu ^a   Kiso, Makoto ^a,c  

^a GIFU UNIVERSITY   (Japan)

^b AICHI UNIVERSITY OF EDUCATION   (Japan)

^c JAPAN SCIENCE AND TECHNOLOGY AGENCY   (Japan)

^d CHUBU UNIVERSITY   (Japan)

^e International Research Center for Infectious Diseases   (Japan)

^f UNIVERSITY OF WISCONSIN MADISON   (United States)

Author keywords

Ab initio FMO; Binding energy; Hemagglutinin; Influenza; Neu5Ac( 2 6)Gal

Indexed keywords

OLIGOSACCHARIDE; RECEPTOR; SIALOSACCHARIDE RECEPTOR; UNCLASSIFIED DRUG; VIRUS HEMAGGLUTININ;

AB INITIO CALCULATION; ARTICLE; BINDING SITE; COMPLEX FORMATION; ENERGY; INFLUENZA VIRUS; LIGAND BINDING; MOLECULAR MODEL; MOLECULAR STABILITY; NONHUMAN; PRIORITY JOURNAL; PROTEIN STRUCTURE; RECEPTOR AFFINITY;

BINDING SITES; CALORIMETRY; CARBOHYDRATE SEQUENCE; HEMAGGLUTININ GLYCOPROTEINS, INFLUENZA VIRUS; HUMANS; OLIGOSACCHARIDES; RECEPTORS, CELL SURFACE;

EID: 33847239926     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2006.12.239     Document Type: Article

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