5NM1

Chicken GRIFIN (crystallisation pH: 6.2)

5NM1 の概要

• エントリーDOI: 10.2210/pdb5nm1/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: galectin related protein, sugar binding protein
• 由来する生物種: Gallus gallus (Chicken)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 66190.83

構造登録者

Ruiz, F.M.,Romero, A. (登録日: 2017-04-05, 公開日: 2018-02-14, 最終更新日: 2024-01-17)

主引用文献

Ruiz, F.M.,Gilles, U.,Ludwig, A.K.,Sehad, C.,Shiao, T.C.,Garcia Caballero, G.,Kaltner, H.,Lindner, I.,Roy, R.,Reusch, D.,Romero, A.,Gabius, H.J.
Chicken GRIFIN: Structural characterization in crystals and in solution.
Biochimie, 146:127-138, 2018

PubMed Abstract: Despite its natural abundance in lenses of vertebrates the physiological function(s) of the galectin-related inter-fiber protein (GRIFIN) is (are) still unclear. The same holds true for the significance of the unique interspecies (fish/birds vs mammals) variability in the capacity to bind lactose. In solution, ultracentrifugation and small angle X-ray scattering (at concentrations up to 9 mg/mL) characterize the protein as compact and stable homodimer without evidence for aggregation. The crystal structure of chicken (C-)GRIFIN at seven pH values from 4.2 to 8.5 is reported, revealing compelling stability. Binding of lactose despite the Arg71Val deviation from the sequence signature of galectins matched the otherwise canonical contact pattern with thermodynamics of an enthalpically driven process. Upon lactose accommodation, the side chain of Arg50 is shifted for hydrogen bonding to the 3-hydroxyl of glucose. No evidence for a further ligand-dependent structural alteration was obtained in solution by measuring hydrogen/deuterium exchange mass spectrometrically in peptic fingerprints. The introduction of the Asn48Lys mutation, characteristic for mammalian GRIFINs that have lost lectin activity, lets labeled C-GRIFIN maintain capacity to stain tissue sections. Binding is no longer inhibitable by lactose, as seen for the wild-type protein. These results establish the basis for detailed structure-activity considerations and are a step to complete the structural description of all seven members of the galectin network in chicken.

PubMed: 29248541
DOI: 10.1016/j.biochi.2017.12.003

実験手法

X-RAY DIFFRACTION (2.099 Å)