6TM2
Human MUC2 AAs 21-1397
Summary for 6TM2
| Entry DOI | 10.2210/pdb6tm2/pdb |
| EMDB information | 10517 |
| Descriptor | Mucin-2, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, CALCIUM ION, ... (7 entities in total) |
| Functional Keywords | glycoprotein, extracellular, polymer, structural protein |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 6 |
| Total formula weight | 307956.03 |
| Authors | Javitt, G.,Khmelnitsky, L.,Albert, L.,Elad, N.,Ilani, T.,Diskin, R.,Fass, D. (deposition date: 2019-12-03, release date: 2020-10-21, Last modification date: 2024-10-23) |
| Primary citation | Javitt, G.,Khmelnitsky, L.,Albert, L.,Bigman, L.S.,Elad, N.,Morgenstern, D.,Ilani, T.,Levy, Y.,Diskin, R.,Fass, D. Assembly Mechanism of Mucin and von Willebrand Factor Polymers. Cell, 183:717-, 2020 Cited by PubMed Abstract: The respiratory and intestinal tracts are exposed to physical and biological hazards accompanying the intake of air and food. Likewise, the vasculature is threatened by inflammation and trauma. Mucin glycoproteins and the related von Willebrand factor guard the vulnerable cell layers in these diverse systems. Colon mucins additionally house and feed the gut microbiome. Here, we present an integrated structural analysis of the intestinal mucin MUC2. Our findings reveal the shared mechanism by which complex macromolecules responsible for blood clotting, mucociliary clearance, and the intestinal mucosal barrier form protective polymers and hydrogels. Specifically, cryo-electron microscopy and crystal structures show how disulfide-rich bridges and pH-tunable interfaces control successive assembly steps in the endoplasmic reticulum and Golgi apparatus. Remarkably, a densely O-glycosylated mucin domain performs an organizational role in MUC2. The mucin assembly mechanism and its adaptation for hemostasis provide the foundation for rational manipulation of barrier function and coagulation. PubMed: 33031746DOI: 10.1016/j.cell.2020.09.021 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.95 Å) |
Structure validation
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