X-ray Crystal Structure of the Human Galectin-3 Carbohydrate Recognition Domain at 2.1- Resolution
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-A resolution. This structure represents the first example of a CRD determined from a galectin which does not show the canonical 2-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.
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关键词：
Animals Humans Galectin 1 Galectin 2 Galectin 3 Antigens, Differentiation Hemagglutinins Crystallography, X-Ray Binding Sites Dimerization
DOI：
10.1074/jbc.273.21.13047
被引量：
年份：
1998
Elsevier
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