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

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

Research output: Contribution to journalArticlepeer-review

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 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.

Original languageEnglish (US)
Pages (from-to)190-196
Number of pages7
JournalFEBS Letters
Volume412
Issue number1
DOIs
StatePublished - Jul 21 1997

Keywords

  • Plant lectin
  • Tn antigen
  • Vicia villosa
  • X-ray crystallography

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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