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Document Figure 4 A CPK model of two tetramers of A/Tokyo/3/67 neuraminidase heads as seen in the crystal structure. The four carbohydrate spikes emanating from the top of the molecule (at Asn146) interdigitate and form an open “barrel” structure. They form an unusual crystal contact. The dark spheres represent carbohydrate and the light spheres represent protein. The carbohydrate at Asn200 starts from one subunit and covers a neighboring subunit on the same tetramer. The other carbohydrates lie on the underside of the tetramer. Page 468 [63,64]. The oligosaccharide appears as a spike emanating from the top of the monomer, forming a crystal contact with a neighboring tetramer in crystals of A/Tokyo/3/67 neuraminidase. The four carbohydrate spikes of a tetramer form an open “barrel” structure of eight carbohydrate chains with the neighboring tetramer, with no apparent intercarbohydrate contacts. This oligosaccharide may play an important but as yet unidentified role in neuraminidase structure or activity. D. Antigenic Variation in Neuraminidase <strong>Structure</strong>s Comparison of all known sequences of approximately 390 residues of the neuraminidase globular head [24], indicates that only 54 (excluding 16 conserved cysteine residues) are invariant (Figure 5a). Apart from 21 residues involved http://legacy.netlibrary.com/nlreader/nlReader.dll?bookid=12640&filename=Page_468.html (1 of 2) [4/9/2004 12:17:07 AM]
Document Figure 5 (a) Stereo image of a CPK atomic model of an influenza virus neuraminidase tetrameric head viewed distal to the viral membrane. The darker-shaded atoms represent totally conserved residues that for the most part form the enzyme active-site pocket. The lighter shaded atoms represent strain-variable residues and carbohydrate. (b) A stereo image of the enzyme active-site pocket of a subunit of neuraminidase with the same shading scheme. Page 469 in preserving the structural integrity of the molecule [46], the main clustering of these invariant residues is within the enzyme active site (Figure 5b), where 17 are in the active site and 16 are neighboring the active site. This is a cavity on the upper surface of the molecule into which sialic acid has been observed to bind [65,66,50]. Excluding the active-site pocket, strain variation occurs over the entire surface of the neuraminidase heads. The active site was found to be in http://legacy.netlibrary.com/nlreader/nlReader.dll?bookid=12640&filename=Page_469.html (1 of 2) [4/9/2004 12:21:29 AM]
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Structure-based Drug Design 14 Stru
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Page 589 and 590: Document Page 476 nM, respectively.
Page 591 and 592: Document Page 478 lished—was asso
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