7P8H

chicken GRIFIN bound to blood group tetrasaccharide B (type 1)

7P8H の概要

• エントリーDOI: 10.2210/pdb7p8h/pdb
• 関連するBIRD辞書のPRD_ID: PRD_002353
• 分子名称: Galectin, alpha-L-fucopyranose-(1-2)-[alpha-D-galactopyranose-(1-3)]beta-D-galactopyranose-(1-3)-2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total)
• 機能のキーワード: grifin, galactoside-binding lectin, blood group b type 1 antigen, beta anomer, sugar binding protein
• 由来する生物種: Gallus gallus (Chicken)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 33794.08

構造登録者

Ruiz, F.M.,Romero, A. (登録日: 2021-07-22, 公開日: 2022-03-02, 最終更新日: 2024-01-31)

主引用文献

Ruiz, F.M.,Medrano, F.J.,Ludwig, A.K.,Kaltner, H.,Shilova, N.V.,Bovin, N.V.,Gabius, H.J.,Romero, A.
Structural Characterization of Rat Galectin-5, an N-Tailed Monomeric Proto-Type-like Galectin.
Biomolecules, 11:-, 2021

PubMed Abstract: Galectins are multi-purpose effectors acting via interactions with distinct counterreceptors based on protein-glycan/protein recognition. These processes are emerging to involve several regions on the protein so that the availability of a detailed structural characterization of a full-length galectin is essential. We report here the first crystallographic information on the N-terminal extension of the carbohydrate recognition domain of rat galectin-5, which is precisely described as an N-tailed proto-type-like galectin. In the ligand-free protein, the three amino-acid stretch from Ser2 to Ser5 is revealed to form an extra β-strand (F0), and the residues from Thr6 to Asn12 are part of a loop protruding from strands S1 and F0. In the ligand-bound structure, amino acids Ser2-Tyr10 switch position and are aligned to the edge of the β-sandwich. Interestingly, the signal profile in our glycan array screening shows the sugar-binding site to preferentially accommodate the histo-blood-group B (type 2) tetrasaccharide and N-acetyllactosamine-based di- and oligomers. The crystal structures revealed the characteristically preformed structural organization around the central Trp77 of the CRD with involvement of the sequence signature's amino acids in binding. Ligand binding was also characterized calorimetrically. The presented data shows that the N-terminal extension can adopt an ordered structure and shapes the hypothesis that a ligand-induced shift in the equilibrium between flexible and ordered conformers potentially acts as a molecular switch, enabling new contacts in this region.

PubMed: 34944498
DOI: 10.3390/biom11121854

実験手法

X-RAY DIFFRACTION (1.13 Å)