4XBN

Crystal Structure of Human Galectin-3 CRD in Complex with Type 1 N-acetyllactosamine

4XBN の概要

• エントリーDOI: 10.2210/pdb4xbn/pdb
• 関連するPDBエントリー: 4XBL 4XBQ
• 分子名称: Galectin-3, beta-D-galactopyranose-(1-3)-2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total)
• 機能のキーワード: complex, human galectin-3 crd, type 1 lacnac, sugar binding protein
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 18255.77

構造登録者

Hsieh, T.J.,Lin, H.Y.,Lin, C.H. (登録日: 2014-12-17, 公開日: 2015-05-20, 最終更新日: 2023-11-08)

主引用文献

Hsieh, T.J.,Lin, H.Y.,Tu, Z.,Huang, B.S.,Wu, S.C.,Lin, C.H.
Structural Basis Underlying the Binding Preference of Human Galectins-1, -3 and -7 for Gal beta 1-3/4GlcNAc.
Plos One, 10:e0125946-e0125946, 2015

PubMed Abstract: Galectins represent β-galactoside-binding proteins and are known to bind Galβ1-3/4GlcNAc disaccharides (abbreviated as LN1 and LN2, respectively). Despite high sequence and structural homology shared by the carbohydrate recognition domain (CRD) of all galectin members, how each galectin displays different sugar-binding specificity still remains ambiguous. Herein we provided the first structural evidence of human galectins-1, 3-CRD and 7 in complex with LN1. Galectins-1 and 3 were shown to have higher affinity for LN2 than for LN1, while galectin-7 displayed the reversed specificity. In comparison with the previous LN2-complexed structures, the results indicated that the average glycosidic torsion angle of galectin-bound LN1 (ψ(LN1) ≈ 135°) was significantly differed from that of galectin-bound LN2 (ψ(LN2 )≈ -108°), i.e. the GlcNAc moiety adopted a different orientation to maintain essential interactions. Furthermore, we also identified an Arg-Asp/Glu-Glu-Arg salt-bridge network and the corresponding loop (to position the second Asp/Glu residue) critical for the LN1/2-binding preference.

PubMed: 25945972
DOI: 10.1371/journal.pone.0125946

実験手法

X-RAY DIFFRACTION (2.208 Å)