5XTS
Crystal structure of the CysR-CTLD3 fragment of human MR at basic/neutral pH
Summary for 5XTS
| Entry DOI | 10.2210/pdb5xts/pdb |
| Descriptor | Macrophage mannose receptor 1, CALCIUM ION (3 entities in total) |
| Functional Keywords | collagen binding, lectin-activity, endocytic receptor, immune receptor, sugar binding protein |
| Biological source | Homo sapiens (Human) |
| Cellular location | Endosome membrane ; Single-pass type I membrane protein : P22897 |
| Total number of polymer chains | 1 |
| Total formula weight | 70579.34 |
| Authors | |
| Primary citation | Hu, Z.,Shi, X.,Yu, B.,Li, N.,Huang, Y.,He, Y. Structural Insights into the pH-Dependent Conformational Change and Collagen Recognition of the Human Mannose Receptor Structure, 26:60-71.e3, 2018 Cited by PubMed Abstract: Mannose receptor (MR, CD206) is an endocytic receptor on microphages and dendritic cells. It recognizes multiple ligands and plays important roles in regulating immune responses and maintaining glycoprotein homeostasis. However, the structure and functional mechanism of MR remain unclear. Here we determine the crystal structures of the N-terminal fragments of MR and reveal the potential binding mode of collagen on the fibronectin II domain. The SAXS and other biophysical data suggest that MR adopts an extended conformation at physiological pH and undergoes conformational changes as pH decreases, resulting in a compact conformation in an acidic environment. Moreover, biochemical data show that MR binds to collagen in a Ca-enhanced manner at physiological pH, whereas Ca has no effect on the binding at acidic pH. These results provide a model for the dynamic mechanism of MR regarding its ligand binding and release during the recycling between cell surface and endosomes. PubMed: 29225077DOI: 10.1016/j.str.2017.11.006 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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