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Journal articles
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.
https://hal-pasteur.archives-ouvertes.fr/pasteur-03136637
Contributor : Marie de TARRAGON Connect in order to contact the contributor
Submitted on : Tuesday, February 9, 2021 - 7:06:17 PM
Last modification on : Thursday, April 7, 2022 - 10:10:54 AM
Contributor : Marie de TARRAGON Connect in order to contact the contributor
Submitted on : Tuesday, February 9, 2021 - 7:06:17 PM
Last modification on : Thursday, April 7, 2022 - 10:10:54 AM
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