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• W2152125983 endingPage "466" @default.
• W2152125983 startingPage "455" @default.
• W2152125983 abstract "Mammalian α1,6-fucosyltransferase (FUT8) catalyses the transfer of a fucose residue from a donor substrate, guanosine 5′-diphosphate-β-l-fucose to the reducing terminal N-acetylglucosamine (GlcNAc) of the core structure of an asparagine-linked oligosaccharide. α1,6-Fucosylation, also referred to as core fucosylation, plays an essential role in various pathophysiological events. Our group reported that FUT8 null mice showed severe growth retardation and emphysema-like lung-destruction as a result of the dysfunction of epidermal growth factor and transforming growth factor-β receptors. To elucidate the molecular basis of FUT8 with respect to pathophysiology, the crystal structure of human FUT8 was determined at 2.6 Å resolution. The overall structure of FUT8 was found to consist of three domains: an N-terminal coiled-coil domain, a catalytic domain, and a C-terminal SH3 domain. The catalytic region appears to be similar to GT-B glycosyltransferases rather than GT-A. The C-terminal part of the catalytic domain of FUT8 includes a Rossmann fold with three regions that are conserved in α1,6-, α1,2-, and protein O-fucosyltransferases. The SH3 domain of FUT8 is similar to other SH3 domain-containing proteins, although the significance of this domain remains to be elucidated. The present findings of FUT8 suggest that the conserved residues in the three conserved regions participate in the Rossmann fold and act as the donor binding site, or in catalysis, thus playing key roles in the fucose-transferring reaction." @default.
• W2152125983 created "2016-06-24" @default.
• W2152125983 creator A5010554991 @default.
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• W2152125983 creator A5081396004 @default.
• W2152125983 creator A5090272663 @default.
• W2152125983 date "2006-12-15" @default.
• W2152125983 modified "2023-10-01" @default.
• W2152125983 title "Crystal structure of mammalian α1,6-fucosyltransferase, FUT8" @default.
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