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The primary structure of the acidic lectin from winged bean ( Psophocarpus tetragonolobus ): insights in carbohydrate recognition, adenine binding and quaternary association
Author(s) -
Srinivas V.R,
Acharya Shreeta,
Rawat Suman,
Sharma Vivek,
Surolia Avadhesha
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)01580-5
Subject(s) - lectin , biology , biochemistry , protein primary structure , peptide sequence , trichosanthin , agglutinin , protein subunit , recombinant dna , conserved sequence , microbiology and biotechnology , gene
The amino acid sequence of the winged bean acidic lectin (WBA II) was determined by chemical means and by recombinant techniques. From the N‐ and C‐terminal sequence, obtained chemically, primers were designed for PCR amplification of the genomic DNA. The PCR product was cloned and sequenced to get the complete primary structure of WBA II. Peptide fragments for sequencing were also obtained by tryptic cleavages of the native lectin. The WBA II sequence showed a high degree of homology with that of WBA I and Erythrina corallodendron lectin (ECorL), especially in the regions involved in subunit association, where there is a very high conservation of residues. This perhaps implies the importance of this particular region in subunit interactions in this lectin. In addition, many of the residues, involved in carbohydrate binding in legume lectins, appear to be conserved in WBA II. The distinct differences in anomeric specificity observed amongst WBA I, WBA II, ECorL and peanut agglutinin (PNA) may be explained by subtle differences in sequence/structure of their D‐loops. WBA II binds adenine quite strongly; a putative adenine binding sequence has been identified.