2ACM

Solution structure of the SEA domain of human mucin 1 (MUC1)

2ACM の概要

• エントリーDOI: 10.2210/pdb2acm/pdb
• 分子名称: Mucin-1 (2 entities in total)
• 機能のキーワード: auto-catalytic proteolysis, structural protein
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Apical cell membrane; Single-pass type I membrane protein. Isoform 5: Secreted. Isoform 7: Secreted. Isoform 9: Secreted. Mucin-1 subunit beta: Cell membrane: Q16615 Q16615
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 13879.25

構造登録者

Macao, B.,Johansson, D.G.A.,Hansson, G.C.,Hard, T. (登録日: 2005-07-19, 公開日: 2006-01-17, 最終更新日: 2024-05-29)

主引用文献

Macao, B.,Johansson, D.G.A.,Hansson, G.C.,Hard, T.
Autoproteolysis coupled to protein folding in the SEA domain of the membrane-bound MUC1 mucin
Nat.Struct.Mol.Biol., 13:71-76, 2006

PubMed Abstract: The single cell layer of the lungs and the gastrointestinal tract is protected by the mucus formed by large glycoproteins called mucins. Transmembrane mucins typically contain 110-residue SEA domains located next to the membrane. These domains undergo post-translational cleavage between glycine and serine in a characteristic GSVVV sequence, but the two peptides remain tightly associated. We show that the SEA domain of the human MUC1 transmembrane mucin undergoes a novel type of autoproteolysis, which is catalyzed by conformational stress and the conserved serine hydroxyl. We propose that self-cleaving SEA domains have evolved to dissociate as a result of mechanical rather than chemical stress at the apical cell membrane and that this protects epithelial cells from rupture. We further suggest that the cell can register mechanical shear at the mucosal surface if the dissociation is signaled via loss of a SEA-binding protein.

PubMed: 16369486
DOI: 10.1038/nsmb1035

実験手法

SOLUTION NMR