Structural studies on peanut lectin complexed with disaccharides involving different linkages: further insights into the structure and interactions of the lectin
Structural studies on peanut lectin complexed with disaccharides involving different linkages: further insights into the structure and interactions of the lectin
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DOI:
10.1107/s0907444906035712
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发表时间:
2006-11-01
影响因子:
2.2
通讯作者:
Vijayan, M.
中科院分区:
文献类型:
--
作者:
Natchiar, S. Kundhavai;Srinivas, O.;Vijayan, M.
Crystal structures of peanut lectin complexed with Gal beta 1-3Gal, methyl-T-antigen, Gal beta 1-6GalNAc, Gal alpha 1-3Gal and Gal alpha 1-6Glc and that of a crystal grown in the presence of Gal alpha 1-3 Gal beta 1-4Gal have been determined using data collected at 100 K. The use of water bridges as a strategy for generating carbohydrate specificity was previously deduced from the complexes of the lectin with lactose (Gal beta 1-4Glc) and T-antigen (Gal beta 1-3GalNAc). This has been confirmed by the analysis of the complexes with Gal beta 1-3Gal and methyl-T-antigen (Gal beta 1-3GalNAc-alpha-OMe). A detailed analysis of lectin-sugar interactions in the complexes shows that they are more extensive when the beta-anomer is involved in the linkage. As expected, the second sugar residue is ill-defined when the linkage is 1 -> 6. There are more than two dozen water molecules which occur in the hydration shells of all structures determined at resolutions better than 2.5 angstrom. Most of them are involved in stabilizing the structure, particularly loops. Water molecules involved in lectin-sugar interactions are also substantially conserved. The lectin molecule is fairly rigid and does not appear to be affected by changes in temperature.