Structural analysis of the jacalin-related lectin MornigaM from the black mulberry (Morus nigra) in complex with mannose.
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.
Rabijns
Anja
A
Laboratory of Analytical Chemistry and Medicinal Physicochemistry, Faculty of Pharmaceutical Sciences, K. U. Leuven, Belgium.
Barre
Annick
A
Van Damme
Els J M
EJ
Peumans
Willy J
WJ
De Ranter
Camiel J
CJ
Rougé
Pierre
P
D000595:Amino Acid Sequence; D001665:Binding Sites; D003116:Color; D018360:Crystallography, X-Ray; D006860:Hydrogen Bonding; D008358:Mannose / Q000737:chemistry / Q000378:metabolism*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D031625:Morus / Q000737:chemistry*; D037121:Plant Lectins / Q000737:chemistry* / Q000378:metabolism*; D020836:Protein Structure, Quaternary; D017434:Protein Structure, Tertiary; D016415:Sequence Alignment
D037121:Plant Lectins; C043696:jacalin; C500656:morniga M; D008358:Mannose