8OV0
MUC5AC CysD7 amino acids 3518-3626
Summary for 8OV0
| Entry DOI | 10.2210/pdb8ov0/pdb |
| Descriptor | Mucin-5AC, CALCIUM ION, CHLORIDE ION, ... (4 entities in total) |
| Functional Keywords | disulfide, mucus, cysd, assembly, structural protein |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 12768.99 |
| Authors | Khmelnitsky, L.,Milo, A.,Dym, O.,Fass, D. (deposition date: 2023-04-25, release date: 2023-08-16, Last modification date: 2024-11-06) |
| Primary citation | Khmelnitsky, L.,Milo, A.,Dym, O.,Fass, D. Diversity of CysD domains in gel-forming mucins. Febs J., 290:5196-5203, 2023 Cited by PubMed Abstract: CysD domains are disulfide-rich modules embedded within long O-glycosylated regions of mucin glycoproteins. CysD domains are thought to mediate intermolecular adhesion during the intracellular bioassembly of mucin polymers and perhaps also after secretion in extracellular mucus hydrogels. The human genome encodes 18 CysD domains distributed across three different mucins. To date, experimental structural information is available only for the first CysD domain (CysD1) of the intestinal mucin MUC2, which is one of the most divergent of the CysDs. To provide experimental data on a CysD that is representative of a larger branch of the fold family, we determined the crystal structure of the seventh CysD domain (CysD7) from MUC5AC, a mucin found in the respiratory tract and stomach. The MUC5AC CysD7 structure revealed a single calcium-binding site, contrasting with the two sites in MUC2 CysD1. The MUC5AC CysD7 structure also contained an additional α-helix absent from MUC2 CysD1, with potential functional implications for intermolecular interactions. Lastly, the experimental structure emphasized the flexibility of the loop analogous to the main adhesion loop of MUC2 CysD1, suggesting that both sequence divergence and physical plasticity in this region may contribute to the adaptation of mucin CysD domains. PubMed: 37526947DOI: 10.1111/febs.16918 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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