Summary for 7LER
| Entry DOI | 10.2210/pdb7ler/pdb |
| Descriptor | Netrin-1, alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total) |
| Functional Keywords | heparin binding protein, filament, signaling protein |
| Biological source | Gallus gallus (Chicken) |
| Total number of polymer chains | 8 |
| Total formula weight | 410860.53 |
| Authors | McDougall, M.,Gupta, M.,Stetefeld, J. (deposition date: 2021-01-14, release date: 2022-02-23, Last modification date: 2024-11-20) |
| Primary citation | Meier, M.,Gupta, M.,Akgul, S.,McDougall, M.,Imhof, T.,Nikodemus, D.,Reuten, R.,Moya-Torres, A.,To, V.,Ferens, F.,Heide, F.,Padilla-Meier, G.P.,Kukura, P.,Huang, W.,Gerisch, B.,Morgelin, M.,Poole, K.,Antebi, A.,Koch, M.,Stetefeld, J. The dynamic nature of netrin-1 and the structural basis for glycosaminoglycan fragment-induced filament formation. Nat Commun, 14:1226-1226, 2023 Cited by PubMed Abstract: Netrin-1 is a bifunctional chemotropic guidance cue that plays key roles in diverse cellular processes including axon pathfinding, cell migration, adhesion, differentiation, and survival. Here, we present a molecular understanding of netrin-1 mediated interactions with glycosaminoglycan chains of diverse heparan sulfate proteoglycans (HSPGs) and short heparin oligosaccharides. Whereas interactions with HSPGs act as platform to co-localise netrin-1 close to the cell surface, heparin oligosaccharides have a significant impact on the highly dynamic behaviour of netrin-1. Remarkably, the monomer-dimer equilibrium of netrin-1 in solution is abolished in the presence of heparin oligosaccharides and replaced with highly hierarchical and distinct super assemblies leading to unique, yet unknown netrin-1 filament formation. In our integrated approach we provide a molecular mechanism for the filament assembly which opens fresh paths towards a molecular understanding of netrin-1 functions. PubMed: 36869049DOI: 10.1038/s41467-023-36692-w PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (5.99 Å) |
Structure validation
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