8EGX
Complex of Fat4(EC1-4) bound to Dchs1(EC1-4)
Summary for 8EGX
| Entry DOI | 10.2210/pdb8egx/pdb |
| Descriptor | Protocadherin Fat 4, Protocadherin-16, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total) |
| Functional Keywords | fat4, dachsous1, cadherin, protocadherin, adhesion, fat, dachsous, cell adhesion |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 2 |
| Total formula weight | 97771.32 |
| Authors | Medina, E.,Luca, V.C. (deposition date: 2022-09-13, release date: 2023-02-22, Last modification date: 2024-11-20) |
| Primary citation | Medina, E.,Easa, Y.,Lester, D.K.,Lau, E.K.,Sprinzak, D.,Luca, V.C. Structure of the planar cell polarity cadherins Fat4 and Dachsous1. Nat Commun, 14:891-891, 2023 Cited by PubMed Abstract: The atypical cadherins Fat and Dachsous are key regulators of cell growth and animal development. In contrast to classical cadherins, which form homophilic interactions to segregate cells, Fat and Dachsous cadherins form heterophilic interactions to induce cell polarity within tissues. Here, we determine the co-crystal structure of the human homologs Fat4 and Dachsous1 (Dchs1) to establish the molecular basis for Fat-Dachsous interactions. The binding domains of Fat4 and Dchs1 form an extended interface along extracellular cadherin (EC) domains 1-4 of each protein. Biophysical measurements indicate that Fat4-Dchs1 affinity is among the highest reported for cadherin superfamily members, which is attributed to an extensive network of salt bridges not present in structurally similar protocadherin homodimers. Furthermore, modeling suggests that unusual extracellular phosphorylation modifications directly modulate Fat-Dachsous binding by introducing charged contacts across the interface. Collectively, our analyses reveal how the molecular architecture of Fat4-Dchs1 enables them to form long-range, high-affinity interactions to maintain planar cell polarity. PubMed: 36797229DOI: 10.1038/s41467-023-36435-x PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.688 Å) |
Structure validation
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