The primary structure of the acidic lectin from winged bean (Psophocarpus tetragonolobus): insights in carbohydrate recognition, adenine binding and quaternary association

FEBS Letters

Acharya, Shreeta¹  Rawat, Suman¹  Srinivas, V.R¹  Sharma, Vivek¹  Surolia, Avadhesha¹ 

[1] Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560012, India

关键词: Lectin;    Primary structure;    Sugar recognition;    WBA I and WBA II;    winged bean basic and acidic agglutinin;    respectively;    PNA;    peanut agglutinin;    ECorL;    Erythrina corallodendron lectin;    IL-IV;    isolectin-IV;    CIP;    calf intestinal phosphatase;   

DOI  :  10.1016/S0014-5793(00)01580-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown