PDBsum entry 3zyj

Cell adhesion

PDB id: 3zyj

Contents

Protein chains

396 a.a.

326 a.a.

Ligands

NAG ×8

BMA

MAN

Metals

_CA ×2

PDB id:

3zyj

Name:

Cell adhesion

Title:

Netring1 in complex with ngl1

Structure:

Leucine-rich repeat-containing protein 4c. Chain: a, c. Fragment: lrr and ig domains, 44-444. Synonym: ngl1, netrin-g1 ligand, ngl-1. Engineered: yes. Netrin-g1. Chain: b, d. Fragment: lam and egf1 domains, 365-783. Synonym: netring1, laminet-1.

Source:

Homo sapiens. Human. Organism_taxid: 9606. Expressed in: homo sapiens. Expression_system_taxid: 9606. Expression_system_cell_line: hek 293 gnti(-).

Resolution:

3.25Å R-factor: 0.257 R-free: 0.268

Authors:

E.Seiradake,C.H.Coles,P.V.Perestenko,K.Harlos,R.A.J.Mcilhinney, A.R.Aricescu,E.Y.Jones

Key ref:

E.Seiradake et al. (2011). Structural basis for cell surface patterning through NetrinG-NGL interactions. Embo J, 30, 4479-4488. PubMed id: 21946559

Date:

23-Aug-11 Release date: 05-Oct-11

Protein chains

Q9HCJ2  (LRC4C_HUMAN) -  Leucine-rich repeat-containing protein 4C from Homo sapiens

Seq: 640 a.a.

Struc: 396 a.a.

Protein chains

Q9Y2I2  (NTNG1_HUMAN) -  Netrin-G1 from Homo sapiens

Seq: 539 a.a.

Struc: 326 a.a.*

* PDB and UniProt seqs differ at 2 residue positions (black crosses)

Embo J 30:4479-4488 (2011)

PubMed id: 21946559

Structural basis for cell surface patterning through NetrinG-NGL interactions.

E.Seiradake, C.H.Coles, P.V.Perestenko, K.Harlos, R.A.McIlhinney, A.R.Aricescu, E.Y.Jones.

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.