1A3K

X-RAY CRYSTAL STRUCTURE OF THE HUMAN GALECTIN-3 CARBOHYDRATE RECOGNITION DOMAIN (CRD) AT 2.1 ANGSTROM RESOLUTION

Summary for 1A3K

• Entry DOI: 10.2210/pdb1a3k/pdb
• Descriptor: GALECTIN-3, beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total)
• Functional Keywords: galectin, galaptin, lectin, ige-binding protein
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 15987.28

Authors

Seetharaman, J.,Kanigsberg, A.,Slaaby, R.,Leffler, H.,Barondes, S.H.,Rini, J.M. (deposition date: 1998-01-22, release date: 1998-07-15, Last modification date: 2024-02-07)

Primary citation

Seetharaman, J.,Kanigsberg, A.,Slaaby, R.,Leffler, H.,Barondes, S.H.,Rini, J.M.
X-ray crystal structure of the human galectin-3 carbohydrate recognition domain at 2.1-A resolution.
J.Biol.Chem., 273:13047-13052, 1998

PubMed Abstract: 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.

PubMed: 9582341
DOI: 10.1074/jbc.273.21.13047

Experimental method

X-RAY DIFFRACTION (2.1 Å)