3ZYJ

NetrinG1 in complex with NGL1

Summary for 3ZYJ

• Entry DOI: 10.2210/pdb3zyj/pdb
• Related: 3ZYI
• Descriptor: LEUCINE-RICH REPEAT-CONTAINING PROTEIN 4C, NETRIN-G1, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total)
• Functional Keywords: cell adhesion, synapse
• Biological source: HOMO SAPIENS (HUMAN); More
• Cellular location: Membrane; Single-pass type I membrane protein: Q9HCJ2; Cell membrane; Lipid-anchor, GPI-anchor (By similarity): Q9Y2I2
• Total number of polymer chains: 4
• Total formula weight: 197408.91

Authors

Seiradake, E.,Coles, C.H.,Perestenko, P.V.,Harlos, K.,McIlhinney, R.A.J.,Aricescu, A.R.,Jones, E.Y. (deposition date: 2011-08-23, release date: 2011-10-05, Last modification date: 2023-12-20)

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

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: 21946559
DOI: 10.1038/EMBOJ.2011.346

Experimental method

X-RAY DIFFRACTION (3.25 Å)