Structural analysis of the jacalin-related lectin MornigaM from the black mulberry (Morus nigra) in complex with mannose |
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Authors: | Rabijns Anja Barre Annick Van Damme Els J M Peumans Willy J De Ranter Camiel J Rougé Pierre |
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Affiliation: | Laboratory of Analytical Chemistry and Medicinal Physicochemistry, Faculty of Pharmaceutical Sciences, K. U. Leuven, Belgium. |
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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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