Cloning and sequencing of winged bean (Psophocarpus tetragonolobus) basic agglutinin (WBA I): presence of second glycosylation site and its implications in quaternary structure.
We report cloning of the DNA encoding winged bean basic agglutinin (WBA I). Using oligonucleotide primers corresponding to N- and C-termini of the mature lectin, the complete coding sequence for WBA I could be amplified from genomic DNA. DNA sequence determination by the chain termination method revealed the absence of any intervening sequences in the gene. The DNA deduced amino acid sequence of WBA I displayed some differences with its primary structure established previously by chemical means. Comparison of the sequence of WBA I with that of other legume lectins highlighted several interesting features, including the existence of the largest specificity determining loop which might account for its oligosaccharide-binding specificity and the presence of an additional N-glycosylation site. These data also throw some light on the relationship between the primary structure of the protein and its probable mode of dimerization.
Sharma
V
V
Molecular Biophysics Unit, Indian Institute of Science, Bangalore, India.
Srinivas
V R
VR
Surolia
A
A
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D001483:Base Sequence; D003001:Cloning, Molecular; D017931:DNA Primers; D006031:Glycosylation; D037102:Lectins / Q000737:chemistry* / Q000235:genetics; D008958:Models, Molecular; D008969:Molecular Sequence Data; D037121:Plant Lectins; D010940:Plant Proteins / Q000737:chemistry*; D016133:Polymerase Chain Reaction; D011487:Protein Conformation; D017386:Sequence Homology, Amino Acid
D000596:Amino Acids; D017931:DNA Primers; D037102:Lectins; D037121:Plant Lectins; D010940:Plant Proteins; C049304:winged bean lectin