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Structural analysis of the jacalin‐related lectin MornigaM from the black mulberry ( Morus nigra ) in complex with mannose
Author(s) -
Rabijns Anja,
Barre Annick,
Van Damme Els J. M.,
Peumans Willy J.,
De Ranter Camiel J.,
Rougé Pierre
Publication year - 2005
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/j.1742-4658.2005.04801.x
Subject(s) - jacalin , mannose , lectin , moraceae , mannan binding lectin , artocarpus , chemistry , biology , biochemistry , botany
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.