Prediction and comparison of the secondary structure of legume lectins.
J Biosci
;
1985 Dec; 9(3&4): 203-212
Article
in English
| IMSEAR
| ID: sea-160495
ABSTRACT
Secondary structure prediction for the 4 legume lectins Concanavalin A, soybean agglutinin, favabean lectin and lentil lectin, was done by the method of Chou and Fasman. This prediction shows that these four lectins fall into a structurally distinct class of proteins, containing high amounts of β-sheet and β-turns. There is a notable similarity in the gross structure of these proteins; all four of them contain about 40–50% of β-sheet, 35–45 % β-turn and 0–10% of α-helix. When the secondary structure of corresponding residues in each pair of these lectins was compared, there was a striking similarity in the Concanavalin A-soybean agglutinin and favabean lectin-lentil lectin pairs, and considerably less similarity in the other pairs, suggesting that these legume lectins have probably evolved in a divergent manner from a common ancestor. A comparison of the predicted potential β-turn sites also supports the hypothesis of divergent evolution in this class of lectins.
Full text:
Available
Index:
IMSEAR (South-East Asia)
Type of study:
Prognostic study
Language:
English
Journal:
J Biosci
Year:
1985
Type:
Article
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