作者
KA Kulkarni, A Srivastava, N Mitra, N Sharon, A Surolia, M Vijayan, K Suguna
发表日期
2004/9/1
期刊
PROTEINS: Structure, Function, and Bioinformatics
卷号
56
期号
4
页码范围
821-827
出版商
Wiley Subscription Services, Inc., A Wiley Company
简介
The three‐dimensional structure of the recombinant form of Erythrina corallodendron lectin, complexed with lactose, has been elucidated by X‐ray crystallography at 2.55 Å resolution. Comparison of this non‐glycosylated structure with that of the native glycosylated lectin reveals that the tertiary and quaternary structures are identical in the two forms, with local changes observed at one of the glycosylation sites (Asn17). These changes take place in such a way that hydrogen bonds with the neighboring protein molecules in rECorL compensate those made by the glycan with the protein in ECorL. Contrary to an earlier report, this study demonstrates that the glycan attached to the lectin does not influence the oligomeric state of the lectin. Identical interactions between the lectin and the non‐covalently bound lactose in the two forms indicate, in line with earlier reports, that glycosylation does not affect the carbohydrate …
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