X-ray crystal structure of the human galectin-3 carbohydrate recognition domain at 2.1-Å resolution

被引:361
作者
Seetharaman, J
Kanigsberg, A
Slaaby, R
Leffler, H
Barondes, SH
Rini, JM [1 ]
机构
[1] Univ Toronto, Dept Mol & Med Genet, Toronto, ON M5S 1A8, Canada
[2] Univ Toronto, Dept Biochem, Toronto, ON M5S 1A8, Canada
[3] Univ Calif San Francisco, Dept Pharmaceut Chem, San Francisco, CA 94143 USA
[4] Univ Calif San Francisco, Dept Psychiat, San Francisco, CA 94143 USA
[5] Univ Calif San Francisco, Dept Neurobiol & Psychiat, San Francisco, CA 94143 USA
关键词
D O I
10.1074/jbc.273.21.13047
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Galectins are a family of lectins which share similar carbohydrate recognition domains (CRDs) and affinity for small beta-galactosides, but which show significant differences in binding specificity for more complex glycoconjugates. We report here the x-ray crystal structure of the human galectin-3 CRD, in complex with lactose and N-acetyllactosamine, at 2.1-Angstrom resolution. This structure represents the first example of a CRD determined from a galectin which does not show the canonical a-fold symmetric dimer organization. Comparison with the published structures of galectins-1 and -2 provides an explanation for the differences in carbohydrate-binding specificity shown by galectin-3, and for the fact that it fails to form dimers by analogous CRD-CRD interactions.
引用
收藏
页码:13047 / 13052
页数:6
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