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

Abstract : 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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Submitted on : Tuesday, February 9, 2021 - 7:06:17 PM
Last modification on : Wednesday, March 31, 2021 - 3:00:22 AM

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Eduardo Osinaga, Diana Tello, Carlos Batthyany, Mario Bianchet, Gisele Tavares, et al.. Amino acid sequence and three-dimensional structure of the Tn-specific isolectin B4 from Vicia villosa. FEBS Letters, Wiley, 1997, 412 (1), pp.190-196. ⟨10.1016/s0014-5793(97)00677-7⟩. ⟨pasteur-03136637⟩

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