7PRL
MUC2 D1 with Cu(II)
Summary for 7PRL
| Entry DOI | 10.2210/pdb7prl/pdb |
| Descriptor | Mucin-2, 2-acetamido-2-deoxy-beta-D-glucopyranose, GLYCEROL, ... (5 entities in total) |
| Functional Keywords | mucin 2, mucin-2, muc2, copper, cu, cu(ii), antimicrobial protein |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 1 |
| Total formula weight | 44128.94 |
| Authors | Reznik, N.,Fass, D. (deposition date: 2021-09-22, release date: 2022-10-26, Last modification date: 2024-11-13) |
| Primary citation | Reznik, N.,Gallo, A.D.,Rush, K.W.,Javitt, G.,Fridmann-Sirkis, Y.,Ilani, T.,Nairner, N.A.,Fishilevich, S.,Gokhman, D.,Chacon, K.N.,Franz, K.J.,Fass, D. Intestinal mucin is a chaperone of multivalent copper. Cell, 185:4206-, 2022 Cited by PubMed Abstract: Mucus protects the epithelial cells of the digestive and respiratory tracts from pathogens and other hazards. Progress in determining the molecular mechanisms of mucus barrier function has been limited by the lack of high-resolution structural information on mucins, the giant, secreted, gel-forming glycoproteins that are the major constituents of mucus. Here, we report how mucin structures we determined enabled the discovery of an unanticipated protective role of mucus: managing the toxic transition metal copper. Using two juxtaposed copper binding sites, one for Cu and the other for Cu, the intestinal mucin, MUC2, prevents copper toxicity by blocking futile redox cycling and the squandering of dietary antioxidants, while nevertheless permitting uptake of this important trace metal into cells. These findings emphasize the value of molecular structure in advancing mucosal biology, while introducing mucins, produced in massive quantities to guard extensive mucosal surfaces, as extracellular copper chaperones. PubMed: 36206754DOI: 10.1016/j.cell.2022.09.021 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.48 Å) |
Structure validation
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