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Cell adhesion/cell adhesion PDB id
3biw
Jmol
Contents
Protein chains
533 a.a. *
177 a.a. *
Ligands
NAG ×12
NAG-NAG ×3
Metals
_CA ×6
* Residue conservation analysis
PDB id:
3biw
Name: Cell adhesion/cell adhesion
Title: Crystal structure of the neuroligin-1/neurexin-1beta synapti complex
Structure: Neuroligin-1. Chain: a, b, c, d. Fragment: extracellular esterase domain of neuroligin-1. Synonym: neuroligin i. Engineered: yes. Neurexin-1-beta. Chain: e, f, g, h. Fragment: extracellular lns domain of neurexin-1beta. Synonym: neurexin i-beta.
Source: Rattus norvegicus. Norway rat. Organism_taxid: 10116. Gene: nlgn1. Expressed in: trichoplusia ni. Expression_system_taxid: 7111. Gene: nrxn1.
Resolution:
3.50Å     R-factor:   0.246     R-free:   0.276
Authors: D.Arac,A.A.Boucard,E.Ozkan,P.Strop,E.Newell,T.C.Sudhof,A.T.B
Key ref: D.Araç et al. (2007). Structures of neuroligin-1 and the neuroligin-1/neurexin-1 beta complex reveal specific protein-protein and protein-Ca2+ interactions. Neuron, 56, 992-1003. PubMed id: 18093522 DOI: 10.1016/j.neuron.2007.12.002
Date:
01-Dec-07     Release date:   18-Dec-07    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q62765  (NLGN1_RAT) -  Neuroligin-1
Seq:
Struc:
 
Seq:
Struc:
843 a.a.
533 a.a.
Protein chains
Pfam   ArchSchema ?
Q63372  (NRX1A_RAT) -  Neurexin-1-alpha
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
1530 a.a.
177 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 3 residue positions (black crosses)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     membrane   1 term 
  Biological process     cell adhesion   1 term 

 

 
DOI no: 10.1016/j.neuron.2007.12.002 Neuron 56:992-1003 (2007)
PubMed id: 18093522  
 
 
Structures of neuroligin-1 and the neuroligin-1/neurexin-1 beta complex reveal specific protein-protein and protein-Ca2+ interactions.
D.Araç, A.A.Boucard, E.Ozkan, P.Strop, E.Newell, T.C.Südhof, A.T.Brunger.
 
  ABSTRACT  
 
Neurexins and neuroligins provide trans-synaptic connectivity by the Ca2+-dependent interaction of their alternatively spliced extracellular domains. Neuroligins specify synapses in an activity-dependent manner, presumably by binding to neurexins. Here, we present the crystal structures of neuroligin-1 in isolation and in complex with neurexin-1 beta. Neuroligin-1 forms a constitutive dimer, and two neurexin-1 beta monomers bind to two identical surfaces on the opposite faces of the neuroligin-1 dimer to form a heterotetramer. The neuroligin-1/neurexin-1 beta complex exhibits a nanomolar affinity and includes a large binding interface that contains bound Ca2+. Alternatively spliced sites in neurexin-1 beta and in neuroligin-1 are positioned nearby the binding interface, explaining how they regulate the interaction. Structure-based mutations of neuroligin-1 at the interface disrupt binding to neurexin-1 beta, but not the folding of neuroligin-1 and confirm the validity of the binding interface of the neuroligin-1/neurexin-1 beta complex. Our results provide molecular insights for understanding the role of cell-adhesion proteins in synapse function.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21155806 G.J.Wright, and P.Washbourne (2011).
Neurexins, neuroligins and LRRTMs: synaptic adhesion getting fishy.
  J Neurochem, 117, 765-778.  
20853446 H.Zhao, S.Xiao, X.Kong, J.Wang, X.Cao, W.Gencheng, H.H.Loh, and P.Y.Law (2011).
Neuron-glial cell communication in the traumatic stress-induced immunomodulation.
  Synapse, 65, 433-440.  
21532576 S.L.Shipman, E.Schnell, T.Hirai, B.S.Chen, K.W.Roche, and R.A.Nicoll (2011).
Functional dependence of neuroligin on a new non-PDZ intracellular domain.
  Nat Neurosci, 14, 718-726.  
20933261 A.Thyagarajan, and A.Y.Ting (2010).
Imaging activity-dependent regulation of neurexin-neuroligin interactions using trans-synaptic enzymatic biotinylation.
  Cell, 143, 456-469.  
20696403 D.Comoletti, M.T.Miller, C.M.Jeffries, J.Wilson, B.Demeler, P.Taylor, J.Trewhella, and T.Nakagawa (2010).
The macromolecular architecture of extracellular domain of alphaNRXN1: domain organization, flexibility, and insights into trans-synaptic disposition.
  Structure, 18, 1044-1053.  
20543817 P.Leone, D.Comoletti, G.Ferracci, S.Conrod, S.U.Garcia, P.Taylor, Y.Bourne, and P.Marchot (2010).
Structural insights into the exquisite selectivity of neurexin/neuroligin synaptic interactions.
  EMBO J, 29, 2461-2471.
PDB code: 2xb6
20519524 T.J.Siddiqui, R.Pancaroglu, Y.Kang, A.Rooyakkers, and A.M.Craig (2010).
LRRTMs and neuroligins bind neurexins with a differential code to cooperate in glutamate synapse development.
  J Neurosci, 30, 7495-7506.  
19553699 F.Carafoli, N.J.Clout, and E.Hohenester (2009).
Crystal structure of the LG1-3 region of the laminin alpha2 chain.
  J Biol Chem, 284, 22786-22792.
PDB code: 2wjs
19730411 J.Ko, C.Zhang, D.Arac, A.A.Boucard, A.T.Brunger, and T.C.Südhof (2009).
Neuroligin-1 performs neurexin-dependent and neurexin-independent functions in synapse validation.
  EMBO J, 28, 3244-3255.  
19660931 P.G.Fuerst, and R.W.Burgess (2009).
Adhesion molecules in establishing retinal circuitry.
  Curr Opin Neurobiol, 19, 389-394.  
19816407 S.H.Lim, S.K.Kwon, M.K.Lee, J.Moon, D.G.Jeong, E.Park, S.J.Kim, B.C.Park, S.C.Lee, S.E.Ryu, D.Y.Yu, B.H.Chung, E.Kim, P.K.Myung, and J.R.Lee (2009).
Synapse formation regulated by protein tyrosine phosphatase receptor T through interaction with cell adhesion molecules and Fyn.
  EMBO J, 28, 3564-3578.  
18812509 C.Reissner, M.Klose, R.Fairless, and M.Missler (2008).
Mutational analysis of the neurexin/neuroligin complex reveals essential and regulatory components.
  Proc Natl Acad Sci U S A, 105, 15124-15129.  
  19360662 K.K.Chadman, S.Gong, M.L.Scattoni, S.E.Boltuck, S.U.Gandhy, N.Heintz, and J.N.Crawley (2008).
Minimal aberrant behavioral phenotypes of neuroligin-3 R451C knockin mice.
  Autism Res, 1, 147-158.  
18667701 K.Mossman, and A.Brunger (2008).
Profile of Axel Brunger.
  Proc Natl Acad Sci U S A, 105, 10643-10645.  
18434543 M.F.Bolliger, J.Pei, S.Maxeiner, A.A.Boucard, N.V.Grishin, and T.C.Südhof (2008).
Unusually rapid evolution of Neuroligin-4 in mice.
  Proc Natl Acad Sci U S A, 105, 6421-6426.  
18974885 S.Biswas, R.J.Russell, C.J.Jackson, M.Vidovic, O.Ganeshina, J.G.Oakeshott, and C.Claudianos (2008).
Bridging the synaptic gap: neuroligins and neurexin I in Apis mellifera.
  PLoS ONE, 3, e3542.  
18923512 T.C.Südhof (2008).
Neuroligins and neurexins link synaptic function to cognitive disease.
  Nature, 455, 903-911.  
18093514 J.N.Levinson, and A.El-Husseini (2007).
A crystal-clear interaction: relating neuroligin/neurexin complex structure to function at the synapse.
  Neuron, 56, 937-939.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.