The structures of MornigaM and the MornigaM-mannose complex have been determined at 1.8 Å and 2.0 Å resolution, respectively. Both structures adopt the typical β-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. © 2005 FEBS.
CITATION STYLE
Rabijns, A., Barre, A., Van Damme, E. J. M., Peumans, W. J., De Ranter, C. J., & Rouge, P. (2005). Structural analysis of the jacalin-related lectin MornigaM from the black mulberry (Morus nigra) in complex with mannose. FEBS Journal, 272(14), 3725–3732. https://doi.org/10.1111/j.1742-4658.2005.04801.x
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