PDBsum entry 3vkf

Cell adhesion

PDB id: 3vkf

Contents

Protein chains

560 a.a.

527 a.a.

177 a.a.

Ligands

NAG-NAG-BMA

NAG ×2

Metals

_CA ×2

PDB id:

3vkf

Name:

Cell adhesion

Title:

Crystal structure of neurexin 1beta/neuroligin 1 complex

Structure:

Neuroligin-1. Chain: a, b. Fragment: acetylcholinesterase-like domain (unp residues 45-638). Synonym: neuroligin i. Engineered: yes. Neurexin-1-beta. Chain: c, d. Fragment: lns domain (unp residues 83-290). Synonym: neurexin i-beta.

Source:

Rattus norvegicus. Rat. Organism_taxid: 10116. Gene: nlgn1. Expressed in: cricetulus griseus. Expression_system_taxid: 10029. Expression_system_cell_line: cho. Bos taurus. Bovine.

Resolution:

3.30Å R-factor: 0.214 R-free: 0.287

Authors:

H.Tanaka,N.Miyazaki,T.Nogi,K.Iwasaki,J.Takagi

Key ref:

H.Tanaka et al. (2012). Higher-order architecture of cell adhesion mediated by polymorphic synaptic adhesion molecules neurexin and neuroligin. Cell Rep, 2, 101-110. PubMed id: 22840401 DOI: 10.1016/j.celrep.2012.06.009

Date:

15-Nov-11 Release date: 01-Aug-12

Protein chain

Q62765  (NLGN1_RAT) -  Neuroligin-1 from Rattus norvegicus

Seq: 843 a.a.

Struc: 560 a.a.

Protein chain

Q62765  (NLGN1_RAT) -  Neuroligin-1 from Rattus norvegicus

Seq: 843 a.a.

Struc: 527 a.a.

Protein chains

Q28142  (NRX1B_BOVIN) -  Neurexin-1-beta from Bos taurus

Seq: 467 a.a.

Struc: 177 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

DOI no: 10.1016/j.celrep.2012.06.009

Cell Rep 2:101-110 (2012)

PubMed id: 22840401

Higher-order architecture of cell adhesion mediated by polymorphic synaptic adhesion molecules neurexin and neuroligin.

H.Tanaka, N.Miyazaki, K.Matoba, T.Nogi, K.Iwasaki, J.Takagi.

ABSTRACT

Polymorphic adhesion molecules neurexin and neuroligin (NL) mediate asymmetric trans-synaptic adhesion, which is crucial for synapse development and function. It is not known whether or how individual synapse function is controlled by the interactions between variants and isoforms of these molecules with differing ectodomain regions. At a physiological concentration of Ca(2+), the ectodomain complex of neurexin-1 β isoform (Nrx1β) and NL1 spontaneously assembled into crystals of a lateral sheet-like superstructure topologically compatible with transcellular adhesion. Correlative light-electron microscopy confirmed extracellular sheet formation at the junctions between Nrx1β- and NL1-expressing non-neuronal cells, mimicking the close, parallel synaptic membrane apposition. The same NL1-expressing cells, however, did not form this higher-order architecture with cells expressing the much longer neurexin-1 α isoform, suggesting a functional discrimination mechanism between synaptic contacts made by different isoforms of neurexin variants.