Abstract
The legume lectins from the subtribe Diocleinae, often referred to as
concanavalin A-like lectins, are a typical example of highly similar
proteins that show distinct biological activities. The pH-dependent
oligomerization that some of these lectins undergo and the relative
position of amino acids within the carbohydrate-binding site are factors
that have been reported to contribute to these differences in the
activities of Diocleinae lectins. In the present work, we determined the
amino acid sequence and the crystal structure of the lectin of Dioclea
rostrata seeds (DRL), with the aim of investigating the structural bases
of the different behavior displayed by this lectin in comparison to
other Diocleinae lectins and determining the reason for the distinct
pH-dependent dimer-tetramer equilibrium. In addition, we discovered a
novel multimeric arrangement for this lectin. (C) 2008 Published by
Elsevier Inc.
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