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Updated: Aug 17, 2026

Rapid Glyco-Qualitative Assessment of Recombinant Proteins Using a Fully Automated System
Published on: June 28, 2024
Structural analysis of the jacalin-related lectin MornigaM from the black mulberry (Morus nigra) in complex with
Anja Rabijns1, Annick Barre, Els J M Van Damme
1Laboratory of Analytical Chemistry and Medicinal Physicochemistry, Faculty of Pharmaceutical Sciences, K. U. Leuven, Belgium.
Abstract:
The structures of MornigaM and the MornigaM-mannose complex have been determined at 1.8 A and 2.0 A resolution, respectively. Both structures adopt the typical beta-prism motif found in other jacalin-related lectins and their tetrameric assembly closely resembles that of jacalin. The carbohydrate-binding cavity of MornigaM readily binds mannose. No major structural rearrangements can be observed in MornigaM upon binding of mannose. These results allow corroboration of the structure-function relationships within the small group of Moraceae lectins.
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