2MK7

Tetra-O-GalNAc glycosylated mucin sequence from alpha dystroglycan mucin domain

2MK7 の概要

• エントリーDOI: 10.2210/pdb2mk7/pdb
• NMR情報: BMRB: 19759
• 分子名称: Alpha-dystroglycan, 2-acetamido-2-deoxy-alpha-D-galactopyranose (2 entities in total)
• 機能のキーワード: mucin domain, glycoprotein, glycosylation, alpha-dystroglycan, tn antigen, n-acetyl-galactosamine, structural 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: 1881.01

構造登録者

Live, D.,Borgert, A. (登録日: 2014-02-02, 公開日: 2015-02-04, 最終更新日: 2024-11-06)

主引用文献

Borgert, A.,Foley, B.L.,Live, D.
Contrasting the conformational effects of alpha-O-GalNAc and alpha-O-Man glycan protein modifications and their impact on the mucin-like region of alpha-dystroglycan.
Glycobiology, 31:649-661, 2021

PubMed Abstract: We have carried out a comparative study of the conformational impact of modifications to threonine residues of either α-O-Man or α-O-GalNAc in the context of a sequence from the mucin-like region of α-dystroglycan. Both such modifications can coexist in this domain of the glycoprotein. Solution NMR experiments and molecular dynamics calculations were employed. Comparing the results for an unmodified peptide Ac- PPTTTTKKP-NH2 sequence from α-dystroglycan, and glycoconjugates with either modification on the Ts, we find that the impact of the α-O-Man modification on the peptide scaffold is quite limited, while that of the α-O-GalNAc is more profound. The results for the α-O-GalNAc glycoconjugate are consistent with what has been seen earlier in other systems. Further examination of the NMR-based structure and the MD results suggest a more extensive network of hydrogen bond interactions within the α-O-GalNAc-threonine residue than has been previously appreciated, which influences the properties of the protein backbone. The conformational effects are relevant to the mechanical properties of α-dystroglycan.

PubMed: 33295623
DOI: 10.1093/glycob/cwaa112

実験手法

SOLUTION NMR