4WVV

Chicken Galectin-8 N-terminal domain complexed with lactose

4WVV の概要

• エントリーDOI: 10.2210/pdb4wvv/pdb
• 関連するBIRD辞書のPRD_ID: PRD_900008
• 分子名称: Galectin, beta-D-galactopyranose-(1-4)-alpha-D-glucopyranose (3 entities in total)
• 機能のキーワード: lectin, carbohydrate recognition domain, sugar binding protein
• 由来する生物種: Gallus gallus (Chicken)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 16980.68

構造登録者

Ruiz, F.M.,Romero, A. (登録日: 2014-11-07, 公開日: 2015-09-23, 最終更新日: 2024-01-10)

主引用文献

Ruiz, F.M.,Gilles, U.,Lindner, I.,Andre, S.,Romero, A.,Reusch, D.,Gabius, H.J.
Combining Crystallography and Hydrogen-Deuterium Exchange to Study Galectin-Ligand Complexes.
Chemistry, 21:13558-13568, 2015

PubMed Abstract: The physiological significance arising from translating information stored in glycans into cellular effects explains the interest in structurally defining lectin-carbohydrate recognition. The relatively small set of adhesion/growth-regulatory galectins in chicken makes this system attractive to study the origins of specificity and divergence. Cell binding by using glycosylation mutants reveals binding of the N-terminal domain of chicken galectin-8 (CG-8N) to α-2,3-sialylated and galactose-terminated glycan chains. Cocrystals with lactose and its 3'-sialylated derivative disclose Arg58 as a key contact for the carboxylic acid and differences in loop lengths to the three homodimeric chicken galectins. Monitoring hydrogen-deuterium exchange by mass spectrometry revealed an effective reduction of deuteration after ligand binding within the contact area. In addition, evidence for changes in solvent accessibility of amide protons beyond this site was obtained. Their detection, which highlights the sensor capacity of this technique, encourages systematic studies on galectins and beyond.

PubMed: 26270612
DOI: 10.1002/chem.201501961

実験手法

X-RAY DIFFRACTION (1.205 Å)