7PRL
MUC2 D1 with Cu(II)
7PRL の概要
| エントリーDOI | 10.2210/pdb7prl/pdb |
| 分子名称 | Mucin-2, 2-acetamido-2-deoxy-beta-D-glucopyranose, GLYCEROL, ... (5 entities in total) |
| 機能のキーワード | mucin 2, mucin-2, muc2, copper, cu, cu(ii), antimicrobial 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 | 44128.94 |
| 構造登録者 | |
| 主引用文献 | 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 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.48 Å) |
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