Weak protein-protein interactions in lectins: the crystal structure of a vegetative lectin from the legume Dolichos biflorus.

TitleWeak protein-protein interactions in lectins: the crystal structure of a vegetative lectin from the legume Dolichos biflorus.
Publication TypeJournal Article
Year of Publication2001
AuthorsButs, L., M-H. Dao-Thi, R. Loris, L. Wyns, M. Etzler, and T. W. Hamelryck
JournalJ Mol Biol
Volume309
Issue1
Pagination193-201
Date Published2001 May 25
ISSN0022-2836
KeywordsAmino Acid Sequence, Amino Acid Substitution, Binding Sites, Carbohydrate Metabolism, Crystallography, X-Ray, Dimerization, Fabaceae, Lectins, Ligands, Models, Molecular, Molecular Sequence Data, Plant Lectins, Plants, Medicinal, Protein Binding, Protein Structure, Quaternary, Protein Structure, Secondary, Sequence Alignment, Structure-Activity Relationship
Abstract

The legume lectins are widely used as a model system for studying protein-carbohydrate and protein-protein interactions. They exhibit a fascinating quaternary structure variation, which becomes important when they interact with multivalent glycoconjugates, for instance those on cell surfaces. Recently, it has become clear that certain lectins form weakly associated oligomers. This phenomenon may play a role in the regulation of receptor crosslinking and subsequent signal transduction. The crystal structure of DB58, a dimeric lectin from the legume Dolichos biflorus reveals a separate dimer of a previously unobserved type, in addition to a tetramer consisting of two such dimers. This tetramer resembles that formed by DBL, the seed lectin from the same plant. A single amino acid substitution in DB58 affects the conformation and flexibility of a loop in the canonical dimer interface. This disrupts the formation of a stable DBL-like tetramer in solution, but does not prohibit its formation in suitable conditions, which greatly increases the possibilities for the cross-linking of multivalent ligands. The non-canonical DB58 dimer has a buried symmetrical alpha helix, which can be present in the crystal in either of two antiparallel orientations. Two existing structures and datasets for lectins with similar quaternary structures were reconsidered. A central alpha helix could be observed in the soybean lectin, but not in the leucoagglutinating lectin from Phaseolus vulgaris. The relative position and orientation of the carbohydrate-binding sites in the DB58 dimer may affect its ability to crosslink mulitivalent ligands, compared to the other legume lectin dimers.

DOI10.1006/jmbi.2001.4639
Alternate JournalJ. Mol. Biol.
PubMed ID11491289