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Volumn 7, Issue 5, 1997, Pages 631-636

New folds of plant lectins

Author keywords

[No Author keywords available]

Indexed keywords

AMARANTH; JACALIN; LECTIN;

EID: 0030823061     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-440X(97)80071-1     Document Type: Article
Times cited : (31)

References (51)
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    • 122). The structure illustrates how large branched oligosaccharides can form supermolecular structures consistent with the crystal symmetry by forming crossbridges between neighboring lectin molecules in the lattice. The mannopentaose binds with high occupancy at two of the binding sites in each subunit. One of these (site 1) has a preference for nonreducing terminal Man and is involved in crossbridge formation, whereas the second one (site 3) is extended and accommodates the whole outer tri-mannose arm of the oligosaccharide. of outstanding interest.
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    • 522) of jacalin (two tetramers per asymmetric unit) complexed with Me-α-D-Gal is determined at 2.4 Å resolution by multiple isomorphous replacement techniques. Each subunit consists of an α chain (133 residues) and a short β chain (20 residues), as a result of proteolysis. Interesting structural features discussed are that the β-prism fold is a new structural fold for plant lectins and representative of all Moraceae lectins. The single binding site per subunit is located at the entrance of the prism fold and has an unusual structure in that the N-terminal amino group of the α chain interacts directly with bound MeGal. of outstanding interest.
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