3ZYO
Crystal structure of the N-terminal leucine rich repeats and immunoglobulin domain of netrin-G ligand-3
Summary for 3ZYO
| Entry DOI | 10.2210/pdb3zyo/pdb |
| Related | 3ZYN |
| Descriptor | LEUCINE-RICH REPEAT-CONTAINING PROTEIN 4B, ZINC ION, 2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total) |
| Functional Keywords | synapse, cell adhesion |
| Biological source | MUS MUSCULUS (HOUSE MOUSE) |
| Cellular location | Membrane; Single-pass membrane protein: P0C192 |
| Total number of polymer chains | 1 |
| Total formula weight | 46724.48 |
| Authors | Seiradake, E.,Coles, C.H.,Perestenko, P.V.,Harlos, K.,McIlhinney, R.A.J.,Aricescu, A.R.,Jones, E.Y. (deposition date: 2011-08-24, release date: 2011-10-05, Last modification date: 2024-11-13) |
| Primary citation | Seiradake, E.,Coles, C.H.,Perestenko, P.V.,Harlos, K.,Mcilhinney, R.A.J.,Aricescu, A.R.,Jones, E.Y. Structural Basis for Cell Surface Patterning Through Netring-Ngl Interactions. Embo J., 30:4479-, 2011 Cited by PubMed Abstract: Brain wiring depends on cells making highly localized and selective connections through surface protein-protein interactions, including those between NetrinGs and NetrinG ligands (NGLs). The NetrinGs are members of the structurally uncharacterized netrin family. We present a comprehensive crystallographic analysis comprising NetrinG1-NGL1 and NetrinG2-NGL2 complexes, unliganded NetrinG2 and NGL3. Cognate NetrinG-NGL interactions depend on three specificity-conferring NetrinG loops, clasped tightly by matching NGL surfaces. We engineered these NGL surfaces to implant custom-made affinities for NetrinG1 and NetrinG2. In a cellular patterning assay, we demonstrate that NetrinG-binding selectivity can direct the sorting of a mixed population of NGLs into discrete cell surface subdomains. These results provide a molecular model for selectivity-based patterning in a neuronal recognition system, dysregulation of which is associated with severe neuropsychological disorders. PubMed: 21946559DOI: 10.1038/EMBOJ.2011.346 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.1 Å) |
Structure validation
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