Glycobiology Advance Access published online on August 25, 2004
Glycobiology, doi:10.1093/glycob/cwh140
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1 Bioinformatics Centre, Indian Institute of Science, Bangalore-560 012, India
* To whom correspondence should be addressed. E-mail: nchandra{at}physics.iisc.ernet.in.
Lectins are known to be important for many biological processes, owing to their ability to recognize cell-surface carbohydrates with high specificity. Plant lectins have been model systems to study protein-carbohydrate recognition, since individually they exhibit high sensitivity and as a group, exhibit large diversity in recognizing carbohydrate structures. While extensive studies have been carried out for legume lectins that have led to interesting insights into the sequence determinants of sugar recognition in them, frameworks with such specific correlations are not available for other plant lectin families. This study reports a large-scale data acquisition and extensive analysis of sequences and structures of
Revised August 19, 2004
Accepted August 20, 2004
ORIGINAL ARTICLES
A database analysis of ‘jacalin-like’ lectins: sequence-structure-function relationships
2 Molecular Biophysics Unit, Indian Institute of Science, Bangalore-560 012, India
Abstract 
-prism-I or ‘jacalin-related lectins’ (JRLs), and shows that hyper-variability in the binding site loops generates carbohydrate recognition diversity, a strategy analogous to that in legume lectins. Analyses of the size, conformation and sequence variability in key regions, reveal the existence of a common theme, encoded as a set of structural features over a common scaffold, in defining specificity. This study also points to the remarkable range of domain architectures, often arising out of gene duplication events in lectins of this family. The data analyzed here also indicates a spectacular variety of quaternary associations possible in this family of lectins that have implications for glycan recognition. These results, thus provide sequence-structure-function correlations, an understanding of the molecular basis of carbohydrate recognition by -prism-I lectins, and also provide a rationale for engineering specific recognition capabilities in relevant molecules.-prism-I fold; carbohydrate recognition.
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