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

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Abstract

Galectins are a family of lectins which share similar carbohydrate recognition domains (CRDs) and affinity for small β-galactosides, but which show significant differences in binding specificity for more complex glyco- conjugates. We report here the x-ray crystal structure of the human galectin- 3 CRD, in complex with lactose and N-acetyllactosamine, at 2.1-Å 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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Seetharaman, J., Kfanigsberg, A., Slaaby, R., Leffler, H., Barondes, S. H., & Rini, J. M. (1998). X-ray crystal structure of the human galectin-3 carbohydrate recognition domain at 2.1-Å resolution. Journal of Biological Chemistry, 273(21), 13047–13052. https://doi.org/10.1074/jbc.273.21.13047

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