3WUC

X-ray crystal structure of Xenopus laevis galectin-Va

Summary for 3WUC

• Entry DOI: 10.2210/pdb3wuc/pdb
• Related: 3WUD
• Related PRD ID: PRD_900008
• Descriptor: Galectin, beta-D-galactopyranose-(1-4)-alpha-D-glucopyranose, MALONIC ACID, ... (4 entities in total)
• Functional Keywords: beta-sandwich, lectin, carbohydrate/sugar binding, sugar binding protein
• Biological source: Xenopus laevis (platanna)
• Total number of polymer chains: 2
• Total formula weight: 32474.60

Authors

Nonaka, Y.,Yoshida, H.,Kamitori, S.,Nakamura, T. (deposition date: 2014-04-23, release date: 2015-04-08, Last modification date: 2023-11-08)

Primary citation

Nonaka, Y.,Ogawa, T.,Yoshida, H.,Shoji, H.,Nishi, N.,Kamitori, S.,Nakamura, T.
Crystal structure of a Xenopus laevis skin proto-type galectin, close to but distinct from galectin-1.
Glycobiology, 25:792-803, 2015

PubMed Abstract: Xenopus laevis (African clawed frog) has two types of proto-type galectins that are similar to mammalian galectin-1 in amino acid sequence. One type, comprising xgalectin-Ia and -Ib, is regarded as being equivalent to galectin-1, and the other type, comprising xgalectin-Va and -Vb, is expected to be a unique galectin subgroup. The latter is considerably abundant in frog skin; however, its biological function remains unclear. We determined the crystal structures of two proto-type galectins, xgalectin-Ib and -Va. The structures showed that both galectins formed a mammalian galectin-1-like homodimer, and furthermore, xgalectin-Va formed a homotetramer. This tetramer structure has not been reported for other galectins. Gel filtration and other experiments indicated that xgalectin-Va was in a dimer-tetramer equilibrium in solution, and lactose binding enhanced the tetramer formation. The residues involved in the dimer-dimer association were conserved in xgalectin-Va and -Vb, and one of the Xenopus (Silurana) tropicalis proto-type galectins, but not in xgalectin-Ia and -Ib, and other galectin-1-equivalent proteins. Xgalectin-Va preferred Galβ1-3GalNAc and not Galβ1-4GlcNAc, while xgalectin-Ib preferred Galβ1-4GlcNAc as well as human galectin-1. Xgalectin-Va/Vb would have diverged from the galectin-1 group with accompanying acquisition of the higher oligomer formation and altered ligand selectivity.

PubMed: 25804418
DOI: 10.1093/glycob/cwv020

Experimental method

X-RAY DIFFRACTION (1.6 Å)