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© Institut Pasteur
Cells infected for 24 hrs with C. Trachomatis. The cell nuclei are labelled in blue, the bacteria appear yellow, within the inclusion lumen. A bacterial protein secreted out the inclusion into the host cytoplasm id labelled in red.
Publication : FEBS letters

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

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in FEBS letters - 21 Jul 1997

Osinaga E, Tello D, Batthyany C, Bianchet M, Tavares G, Durán R, Cerveñansky C, Camoin L, Roseto A, Alzari PM

Link to Pubmed [PMID] – 9257718

FEBS Lett. 1997 Jul;412(1):190-6

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.

http://www.ncbi.nlm.nih.gov/pubmed/9257718