1GAN

COMPLEX OF TOAD OVARY GALECTIN WITH N-ACETYLGALACTOSE

1GAN の概要

• エントリーDOI: 10.2210/pdb1gan/pdb
• 関連するBIRD辞書のPRD_ID: PRD_900019
• 分子名称: GALECTIN-1, beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-alpha-D-glucopyranose (3 entities in total)
• 機能のキーワード: s-lectin, carbohydrate binding, lectin
• 由来する生物種: Bufo arenarum
• 細胞内の位置: Secreted, extracellular space, extracellular matrix: P56217
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 30161.99

構造登録者

Amzel, L.M.,Bianchet, M.A.,Ahmed, H.,Vasta, G.R. (登録日: 1996-11-06, 公開日: 1997-09-04, 最終更新日: 2024-05-22)

主引用文献

Bianchet, M.A.,Ahmed, H.,Vasta, G.R.,Amzel, L.M.
Soluble beta-galactosyl-binding lectin (galectin) from toad ovary: crystallographic studies of two protein-sugar complexes.
Proteins, 40:378-388, 2000

PubMed Abstract: Galectin-1, S-type beta-galactosyl-binding lectins present in vertebrate and invertebrate species, are dimeric proteins that participate in cellular adhesion, activation, growth regulation, and apoptosis. Two high-resolution crystal structures of B. arenarum galectin-1 in complex with two related carbohydrates, LacNAc and TDG, show that the topologically equivalent hydroxyl groups in the two disaccharides exhibit identical patterns of interaction with the protein. Groups that are not equivalent between the two sugars present in the second moiety of the disaccharide, interact differently with the protein, but use the same number and quality of interactions. The structures show additional protein-carbohydrate interactions not present in previously reported lectin-lactose complexes. These contacts provide an explanation for the enhanced affinity of galectin-1 for TDG and LacNAc relative to lactose. Galectins are in dimer-monomer equilibrium at physiological protein concentrations, suggesting that this equilibrium may be involved in organ-specific regulation of activity. Comparison of B. arenarum with other galectin-1 structures shows that among different galectins there are significant changes in accessible surface area buried upon dimer formation, providing a rationale for the variations observed in the free-energies of dimerization. The structure of the B. arenarum galectin-1 has a large cleft with a strong negative potential that connects the two binding sites at the surface of the protein. Such a striking characteristic suggests that this cleft is probably involved in interactions of the galectin with other intra or extra-cellular proteins. Proteins 2000;40:378-388.

PubMed: 10861929
DOI: 10.1002/1097-0134(20000815)40:3<378::AID-PROT40>3.0.CO;2-7

実験手法

X-RAY DIFFRACTION (2.23 Å)