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

doi:10.1016/S0014-5793(97)00677-7

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

School of Medicine

Research output: Contribution to journal › Article › peer-review

26 Scopus citations

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 language	English (US)
Pages (from-to)	190-196
Number of pages	7
Journal	FEBS Letters
Volume	412
Issue number	1
DOIs	https://doi.org/10.1016/S0014-5793(97)00677-7
State	Published - 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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10.1016/S0014-5793(97)00677-7

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title = "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 {\AA} 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.",

keywords = "Plant lectin, Tn antigen, Vicia villosa, X-ray crystallography",

author = "Eduardo Osinaga and Diana Tello and Carlos Batthyany and Mario Bianchet and Gisele Tavares and Rosario Dur{\'a}n and Carlos Cerve{\~n}ansky and Luc Camoin and Alberto Roseto and Alzari, {Pedro M.}",

note = "Funding Information: We are grateful to Frederick Saul for helpful discussions. This work was partially supported by grants from CONICYT-BID, Institut Pasteur (Paris), La Ligue contre le Cancer, ECOS France-Uruguay Program, Comisi{\'o}n Honoraria de Lucha contra el Cancer (Uruguay) and CSIC (Universidad de la Rep{\'u}blica, Uruguay). Gisele Tavares was supported by a grant from the Brazilian National Research Council CNPq.",

year = "1997",

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doi = "10.1016/S0014-5793(97)00677-7",

language = "English (US)",

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T1 - Amino acid sequence and three-dimensional structure of the Tn-specific isolectin B4 from Vicia villosa

AU - Osinaga, Eduardo

AU - Tello, Diana

AU - Batthyany, Carlos

AU - Bianchet, Mario

AU - Tavares, Gisele

AU - Durán, Rosario

AU - Cerveñansky, Carlos

AU - Camoin, Luc

AU - Roseto, Alberto

AU - Alzari, Pedro M.

N1 - Funding Information: We are grateful to Frederick Saul for helpful discussions. This work was partially supported by grants from CONICYT-BID, Institut Pasteur (Paris), La Ligue contre le Cancer, ECOS France-Uruguay Program, Comisión Honoraria de Lucha contra el Cancer (Uruguay) and CSIC (Universidad de la República, Uruguay). Gisele Tavares was supported by a grant from the Brazilian National Research Council CNPq.

PY - 1997/7/21

Y1 - 1997/7/21

N2 - 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.

AB - 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.

KW - Plant lectin

KW - Tn antigen

KW - Vicia villosa

KW - X-ray crystallography

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

Abstract

Keywords

ASJC Scopus subject areas

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