2acm
From Proteopedia
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| Gene: | MUC1 (Homo sapiens) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Solution structure of the SEA domain of human mucin 1 (MUC1)
Overview
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.
About this Structure
2ACM is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Autoproteolysis coupled to protein folding in the SEA domain of the membrane-bound MUC1 mucin., Macao B, Johansson DG, Hansson GC, Hard T, Nat Struct Mol Biol. 2006 Jan;13(1):71-6. Epub 2005 Dec 20. PMID:16369486
Page seeded by OCA on Mon Mar 31 01:50:47 2008
