8OV0

MUC5AC CysD7 amino acids 3518-3626

8OV0 の概要

• エントリーDOI: 10.2210/pdb8ov0/pdb
• 分子名称: Mucin-5AC, CALCIUM ION, CHLORIDE ION, ... (4 entities in total)
• 機能のキーワード: disulfide, mucus, cysd, assembly, 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: 12768.99

構造登録者

Khmelnitsky, L.,Milo, A.,Dym, O.,Fass, D. (登録日: 2023-04-25, 公開日: 2023-08-16, 最終更新日: 2024-11-06)

主引用文献

Khmelnitsky, L.,Milo, A.,Dym, O.,Fass, D.
Diversity of CysD domains in gel-forming mucins.
Febs J., 290:5196-5203, 2023

PubMed Abstract: CysD domains are disulfide-rich modules embedded within long O-glycosylated regions of mucin glycoproteins. CysD domains are thought to mediate intermolecular adhesion during the intracellular bioassembly of mucin polymers and perhaps also after secretion in extracellular mucus hydrogels. The human genome encodes 18 CysD domains distributed across three different mucins. To date, experimental structural information is available only for the first CysD domain (CysD1) of the intestinal mucin MUC2, which is one of the most divergent of the CysDs. To provide experimental data on a CysD that is representative of a larger branch of the fold family, we determined the crystal structure of the seventh CysD domain (CysD7) from MUC5AC, a mucin found in the respiratory tract and stomach. The MUC5AC CysD7 structure revealed a single calcium-binding site, contrasting with the two sites in MUC2 CysD1. The MUC5AC CysD7 structure also contained an additional α-helix absent from MUC2 CysD1, with potential functional implications for intermolecular interactions. Lastly, the experimental structure emphasized the flexibility of the loop analogous to the main adhesion loop of MUC2 CysD1, suggesting that both sequence divergence and physical plasticity in this region may contribute to the adaptation of mucin CysD domains.

PubMed: 37526947
DOI: 10.1111/febs.16918

実験手法

X-RAY DIFFRACTION (1.7 Å)