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This article describes the crystal structure of influenza virus neuraminidase, information about the active site which may lead to development of specific and effective inhibitors of the enzyme, and the structure of epitopes (antigenic determinants) on the neuraminidase. The 3\u2010dimensional structure of the epitopes was obtained by X\u2010ray diffraction methods using crystals of neuraminidase complexed with monoclonal antibody Fab fragments. Escape mutants, selected by growing virus in the presence of monoclonal antibodies to the neuraminidase, possess single amino acid sequence changes. The crystal structure of two mutants showed that the change in structure was restricted to that particular sidechain, but the change in the epitope was sufficient to abolish antibody binding even though it is known in one case that 21 other amino acids on the neuraminidase are in contact with the antibody.<\/jats:p>","DOI":"10.1002\/prot.340060402","type":"journal-article","created":{"date-parts":[[2005,5,29]],"date-time":"2005-05-29T01:03:53Z","timestamp":1117328633000},"page":"341-356","source":"Crossref","is-referenced-by-count":260,"title":["The neuraminidase of influenza virus"],"prefix":"10.1002","volume":"6","author":[{"given":"Gillian M.","family":"Air","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"W. 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