Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

3ZYG

NETRING2 LAM AND EGF1 DOMAINS

Summary for 3ZYG
Entry DOI10.2210/pdb3zyg/pdb
Related3ZYI 3ZYJ
DescriptorNETRIN-G2, 2-acetamido-2-deoxy-beta-D-glucopyranose, CALCIUM ION, ... (4 entities in total)
Functional Keywordscell adhesion, synapse
Biological sourceHOMO SAPIENS (HUMAN)
Cellular locationCell membrane; Lipid-anchor, GPI-anchor (By similarity): Q96CW9
Total number of polymer chains2
Total formula weight82335.37
Authors
Seiradake, E.,Coles, C.H.,Perestenko, P.V.,Harlos, K.,Mcilhinney, R.A.J.,Aricescu, A.R.,Jones, E.Y. (deposition date: 2011-08-22, release date: 2011-10-05, Last modification date: 2024-11-06)
Primary citationSeiradake, 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: 21946559
DOI: 10.1038/EMBOJ.2011.346
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.2 Å)
Structure validation

231029

건을2025-02-05부터공개중

PDB statisticsPDBj update infoContact PDBjnumon