PDBsum entry 3poy

Cell adhesion

PDB id: 3poy

Contents

Protein chain

1005 a.a.

Ligands

NAG-NAG-BMA

BGC

Waters ×33

PDB id:

3poy

Name:

Cell adhesion

Title:

Crystal structure of the alpha-neurexin-1 ectodomain, lns 2-6

Structure:

Neurexin-1-alpha. Chain: a. Fragment: ectodomain (unp residues 296-1349). Engineered: yes. Mutation: yes

Source:

Bos taurus. Bovine. Organism_taxid: 9913. Gene: nrxn1. Expressed in: homo sapiens. Expression_system_taxid: 9606. Expression_system_cell_line: hek293s gnt1-.

Resolution:

3.02Å R-factor: 0.216 R-free: 0.269

Authors:

M.T.Miller,M.Mileni,D.Comoletti,R.C.Stevens,M.Harel,P.Taylor

Key ref:

M.T.Miller et al. (2011). The crystal structure of the α-neurexin-1 extracellular region reveals a hinge point for mediating synaptic adhesion and function. Structure, 19, 767-778. PubMed id: 21620717

Date:

23-Nov-10 Release date: 08-Jun-11

Protein chain

Q28146  (NRX1A_BOVIN) -  Neurexin-1 from Bos taurus

Seq: 1530 a.a.

Struc: 1005 a.a.*

* PDB and UniProt seqs differ at 7 residue positions (black crosses)

Structure 19:767-778 (2011)

PubMed id: 21620717

The crystal structure of the α-neurexin-1 extracellular region reveals a hinge point for mediating synaptic adhesion and function.

M.T.Miller, M.Mileni, D.Comoletti, R.C.Stevens, M.Harel, P.Taylor.

ABSTRACT

α- and β-neurexins (NRXNs) are transmembrane cell adhesion proteins that localize to presynaptic membranes in neurons and interact with the postsynaptic neuroligins (NLGNs). Their gene mutations are associated with the autism spectrum disorders. The extracellular region of α-NRXNs, containing nine independently folded domains, has structural complexity and unique functional characteristics, distinguishing it from the smaller β-NRXNs. We have solved the X-ray crystal structure of seven contiguous domains of the α-NRXN-1 extracellular region at 3.0 Å resolution. The structure reveals an arrangement where the N-terminal five domains adopt a more rigid linear conformation and the two C-terminal domains form a separate arm connected by a flexible hinge. In an extended conformation the molecule is suitably configured to accommodate a bound NLGN molecule, as supported by structural comparison and surface plasmon resonance. These studies provide the structural basis for a multifunctional synaptic adhesion complex mediated by α-NRXN-1.