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Amino acid sequence and three‐dimensional structure of the Tn‐specific isolectin B4 from Vicia villosa
Author(s) -
Osinaga Eduardo,
Tello Diana,
Batthyany Carlos,
Bianchet Mario,
Tavares Gisele,
Durán Rosario,
Cerveñansky Carlos,
Camoin Luc,
Roseto Alberto,
Alzari Pedro M
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)00677-7
Subject(s) - vicia villosa , protein quaternary structure , glycopeptide , villosa , amino acid , chemistry , peptide , peptide sequence , biochemistry , protein subunit , stereochemistry , glycosylation , lectin , biology , genetics , gene , cover crop , agronomy , antibiotics
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 Å resolution to a crystallographic R ‐factor of 21%. Each subunit displays the thirteen‐stranded β‐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.