Molecular modeling of sialyloligosaccharide fragments into the active site of influenza virus N9 neuraminidase.
Molecular modeling studies have been carried out to investigate the interactions between substrate sialyloligosaccharide (SOS) fragments bearing different glycosidic linkages and influenza virus N9 neuraminidase, a surface glycoprotein of influenza virus subtype N9. The studies revealed that the allowed orientation for sialic acid (SA) is less than 1% in the Eulerian space at the active site. The active site of this enzyme has enough space to accommodate various SOS fragments, NeuNAcalpha(2-3)Gal, NeuNAcalpha(2-6)Gal, NeuNAcalpha(2-8)NeuNAc and NeuNAcalpha(2-9)NeuNAc, but on specific conformations. In the bound conformation, among these substrates there exists a conformational similarity leading to a structural similarity, which may be an essential requirement for the cleavage activity of the neuraminidases irrespective of the type of glycosidic linkage.
Veluraja
K
K
Department of Physics, Manonmaniam Sundaranar University, Tirunelveli, India. bio@md3.vsnl.net.in
Suresh
M X
MX
Christlet
T H
TH
Rafi
Z A
ZA
D002236:Carbohydrate Conformation; D002240:Carbohydrate Sequence; D020134:Catalytic Domain; D003198:Computer Simulation; D006860:Hydrogen Bonding; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009439:Neuraminidase / Q000737:chemistry* / Q000378:metabolism*; D009844:Oligosaccharides / Q000737:chemistry* / Q000378:metabolism*; D009975:Orthomyxoviridae / Q000201:enzymology*; D011487:Protein Conformation; D013379:Substrate Specificity; D013816:Thermodynamics
D009844:Oligosaccharides; C016735:sialooligosaccharides; D009439:Neuraminidase