The Mannose-specific bulb lectin from Galanthus nivalis (snowdrop) binds mono- and dimannosides at distinct sites. Structure analysis of refined complexes at 2.3 angstrom and 3.0 angstrom resolution
The Mannose-specific bulb lectin from Galanthus nivalis (snowdrop) binds mono- and dimannosides at distinct sites. Structure analysis of refined complexes at 2.3 angstrom and 3.0 angstrom resolution
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DOI:
10.1006/jmbi.1996.0532
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发表时间:
1996-10-04
影响因子:
5.6
通讯作者:
Wright, CS
中科院分区:
文献类型:
--
作者:
Hester, G;Wright, CS
Galanthus nivalis agglutinin (GNA, a 50 kDa tetramer) is a mannose-specific lectin of the Amaryllidaceae family of bulb lectins. Crystal structures of GNA complexed with methyl-alpha-D-mannose (MeMan) and mannose-alpha 1,3-D-mannose-alpha-OMe (MeMan-2) have been determined and analyzed in terms of internal structural symmetry and saccharide binding. The final model of the 2.29 Angstrom orthorhombic methyl-alpha-Man complex refined with an X-factor of 0.167 (all data) includes 12 bound sugar ligands and 327 water molecules. The four independent subunits (A, B, C and D) of the 222 tetramer and the three four-stranded beta-sheets (I,II and III) that constitute each subunit compare closely (r.m.s.Delta =