PubMed:11588153 JSONTXT

{"target":"https://pubannotation.org/docs/sourcedb/PubMed/sourceid/11588153","sourcedb":"PubMed","sourceid":"11588153","source_url":"http://www.ncbi.nlm.nih.gov/pubmed/11588153","text":"Fucosyltransferases: structure/function studies.\nAlpha3-fucosyltransferases (alpha3-FucTs) catalyze the final step in the synthesis of a range of important glycoconjugates that function in cell adhesion and lymphocyte recirculation. Six members of this family of enzymes have been cloned from the human genome, and their expression pattern has been shown to be highly regulated. Each enzyme has a unique acceptor substrate binding pattern, and each generates a unique range of fucosylated products. Results from a range of studies have provided information on amino acids in the FucT sequence that contribute to the differential acceptor specificity for the FucTs, and to the binding of the nucleotide sugar donor GDP-fucose. These results, in conjunction with results obtained from the analysis of the disulfide bond pattern, have provided useful clues about the spatial distribution of amino acids that influence or directly contribute to substrate binding. This information is reviewed here, and a molecular fold prediction is presented which has been constructed based on the available information and current modeling 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