Glycobiology Advance Access originally published online on June 8, 2005
Glycobiology 2005 15(10):1033-1042; doi:10.1093/glycob/cwi088
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Crystal structure of banana lectin reveals a novel second sugar binding site
2 Life Sciences Institute, University of Michigan, Ann Arbor, MI; and 3 Department of Biological Chemistry, University of Michigan Medical School, Ann Arbor, MI
1 To whom correspondence should be addressed; e-mail: jass{at}umich.edu
Received on May 4, 2005; revised on May 17, 2005; accepted on June 1, 2005
Banana lectin (Banlec) is a dimeric plant lectin from the jacalin-related lectin family. Banlec belongs to a subgroup of this family that binds to glucose/mannose, but is unique in recognizing internal 
1,3 linkages as well as ß1,3 linkages at the reducing termini. Here we present the crystal structures of Banlec alone and with laminaribiose (LAM) (Glcß1, 3Glc) and Xyl-ß1,3-Man--O-Methyl. The structure of Banlec has a ß-prism-I fold, similar to other family members, but differs from them in its mode of sugar binding. The reducing unit of the sugar is inserted into the binding site causing the second saccharide unit to be placed in the opposite orientation compared with the other ligand-bound structures of family members. More importantly, our structures reveal the presence of a second sugar binding site that has not been previously reported in the literature. The residues involved in the second site are common to other lectins in this family, potentially signaling a new group of mannose-specific jacalin-related lectins (mJRL) with two sugar binding sites.
Key words: banana lectin / laminaribiose / mannose-specific jacalin-related lectin
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