6ZSY
Crystal structure of the Grindelwald extracellular domain complex
Summary for 6ZSY
| Entry DOI | 10.2210/pdb6zsy/pdb |
| Descriptor | Protein grindelwald (2 entities in total) |
| Functional Keywords | tnf receptor, jnk cascade, tnf, signaling, extracellular, tumor necrosis factor, signaling protein |
| Biological source | Drosophila melanogaster (Fruit fly) |
| Total number of polymer chains | 1 |
| Total formula weight | 5919.62 |
| Authors | Palmerini, V.,Cecatiello, V.,Pasqualato, S.,Mapelli, M. (deposition date: 2020-07-17, release date: 2021-03-31, Last modification date: 2024-11-13) |
| Primary citation | Palmerini, V.,Monzani, S.,Laurichesse, Q.,Loudhaief, R.,Mari, S.,Cecatiello, V.,Olieric, V.,Pasqualato, S.,Colombani, J.,Andersen, D.S.,Mapelli, M. Drosophila TNFRs Grindelwald and Wengen bind Eiger with different affinities and promote distinct cellular functions. Nat Commun, 12:2070-2070, 2021 Cited by PubMed Abstract: The Drosophila tumour necrosis factor (TNF) ligand-receptor system consists of a unique ligand, Eiger (Egr), and two receptors, Grindelwald (Grnd) and Wengen (Wgn), and therefore provides a simple system for exploring the interplay between ligand and receptors, and the requirement for Grnd and Wgn in TNF/Egr-mediated processes. Here, we report the crystallographic structure of the extracellular domain (ECD) of Grnd in complex with Egr, a high-affinity hetero-hexameric assembly reminiscent of human TNF:TNFR complexes. We show that ectopic expression of Egr results in internalisation of Egr:Grnd complexes in vesicles, a step preceding and strictly required for Egr-induced apoptosis. We further demonstrate that Wgn binds Egr with much reduced affinity and is localised in intracellular vesicles that are distinct from those containing Egr:Grnd complexes. Altogether, our data provide insight into ligand-mediated activation of Grnd and suggest that distinct affinities of TNF ligands for their receptors promote different and non-redundant cellular functions. PubMed: 33824334DOI: 10.1038/s41467-021-22080-9 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (0.926 Å) |
Structure validation
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