title: Computational studies of H5N1 hemagglutinin binding with SA-alpha-2, 3-Gal and SA-alpha-2, 6-Gal.
abstract: For influenza H5N1 hemagglutinin, a switch from SA-alpha-2, 3-Gal to SA-alpha-2, 6-Gal receptor specificity is a critical step leading to the conversion from avian-to-human to human-to-human infection. Therefore, the understanding of the binding modes of SA-alpha-2, 3-Gal and SA-alpha-2, 6-Gal to H5N1 hemagglutinin will be very important for the examination of possible mutations needed for going from an avian to a human flu virus. Based on the available H5N1 hemagglutinin crystal structure, the binding profiles between H5N1 hemagglutinin and two saccharide ligands, SA-alpha-2, 3-Gal and SA-alpha-2, 6-Gal, were investigated by ab initio quantum mechanics, molecular docking, molecular mechanics, and molecular dynamics simulations. It was found that SA-alpha-2, 3-Gal has strong multiple hydrophobic and hydrogen bond interactions in its trans conformation with H5N1 hemagglutinin, whereas the SA-alpha-2, 6-Gal only shows weak interactions in a different conformation (cis type).
authors.affiliation: Department of Chemistry and Center for Biotechnology and Drug Design, Georgia State University, Atlanta, 30302-4098, USA.
authors.forename: Minyong
authors.initials: M
authors.lastname: Li
authors.forename: Binghe
authors.initials: B
authors.lastname: Wang
mesh_terms: D019295:Computational Biology; D005690:Galactose / Q000737:chemistry* / Q000378:metabolism*; D019267:Hemagglutinin Glycoproteins, Influenza Virus / Q000737:chemistry* / Q000378:metabolism*; D053124:Influenza A Virus, H5N1 Subtype / Q000378:metabolism*; D008958:Models, Molecular; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D012794:Sialic Acids / Q000737:chemistry* / Q000378:metabolism*; D040681:Structural Homology, Protein
chemical_list: D019267:Hemagglutinin Glycoproteins, Influenza Virus; D012794:Sialic Acids; D005690:Galactose