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Amino acid sequence and three-dimensional structure of the Tn-specific isolectin B4 from Vicia villosa

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Osinaga, Eduardo | Tello, Diana | Batthyany, Carlos | Bianchet, Mario | Tavares, Gisele | Durán, Rosario | Cerveñansky, Carlos | Camoin, Luc | Roseto, Alberto | Alzari, Pedro

Edité par CCSD ; Wiley -

International audience. The partial amino acid sequence of the tetrameric isolectin B4 from Vicia villosa seeds has been determined by peptide analysis, and its three-dimensional structure solved by molecular replacement techniques and refined at 2.9 A resolution to a crystallographic R-factor of 21%. Each subunit displays the thirteen-stranded beta-barrel topology characteristic of legume lectins. The amino acid residues involved in metal- and sugar-binding are similar to those of other GalNAc-specific lectins, indicating that residues outside the carbohydrate-binding pocket modulate the affinity for the Tn glycopeptide. Isolectin B4 displays an unusual quaternary structure, probably due to protein glycosylation.

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