Assessment | Biopsychology | Comparative | Cognitive | Developmental | Language | Individual differences | Personality | Philosophy | Social |
Methods | Statistics | Clinical | Educational | Industrial | Professional items | World psychology |

Biological: Behavioural genetics · Evolutionary psychology · Neuroanatomy · Neurochemistry · Neuroendocrinology · Neuroscience · Psychoneuroimmunology · Physiological Psychology · Psychopharmacology (Index, Outline)


Neurexin-1-alpha is a protein that in humans is encoded by the NRXN1 gene.[1]

Neurexins are a family of proteins that function in the vertebrate nervous system as cell adhesion molecules and receptors. They are encoded by several unlinked genes of which two, NRXN1 and NRXN3, are among the largest known human genes. Three of the genes (NRXN1-3) utilize two alternate promoters and include numerous alternatively spliced exons to generate thousands of distinct mRNA transcripts and protein isoforms. The majority of transcripts are produced from the upstream promoter and encode alpha-neurexin isoforms; a much smaller number of transcripts are produced from the downstream promoter and encode beta-neurexin isoforms. The alpha-neurexins contain epidermal growth factor-like (EGF-like) sequences and laminin G domains, and have been shown to interact with neurexophilins. The beta-neurexins lack EGF-like sequences and contain fewer laminin G domains than alpha-neurexins.[1]


The gene is found in a single copy on the short arm of chromosome 2 (2p16.3). The gene is 1,112,187 bases in length, is located on the Crick (minus) strand and encodes a protein of 1,477 amino acids (molecular weight 161.883 kDa).


NRXN1 has been shown to interact with NLGN1.[2][3]


  1. 1.0 1.1 Entrez Gene: NRXN1 neurexin 1.
  2. Comoletti, Davide, Flynn Robyn, Jennings Lori L, Chubykin Alexander, Matsumura Takehito, Hasegawa Hana, Südhof Thomas C, Taylor Palmer (Dec. 2003). Characterization of the interaction of a recombinant soluble neuroligin-1 with neurexin-1beta. J. Biol. Chem. 278 (50): 50497–50505.
  3. Ichtchenko, K, Nguyen T, Südhof T C (Feb. 1996). Structures, alternative splicing, and neurexin binding of multiple neuroligins. J. Biol. Chem. 271 (5): 2676–2682.

Further readingEdit

  • Missler M, Südhof TC (1998). Neurexins: three genes and 1001 products. Trends Genet. 14 (1): 20–26.
  • Nakajima D (2003). Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones. DNA Res. 9 (3): 99–106.
  • Ushkaryov YA, Petrenko AG, Geppert M, Südhof TC (1992). Neurexins: synaptic cell surface proteins related to the alpha-latrotoxin receptor and laminin. Science 257 (5066): 50–56.
  • Ichtchenko K, Nguyen T, Südhof TC (1996). Structures, alternative splicing, and neurexin binding of multiple neuroligins. J. Biol. Chem. 271 (5): 2676–2682.
  • Petrenko AG (1996). Structure and evolution of neurexophilin. J. Neurosci. 16 (14): 4360–9.
  • Hata Y, Butz S, Südhof TC (1996). CASK: a novel dlg/PSD95 homolog with an N-terminal calmodulin-dependent protein kinase domain identified by interaction with neurexins. J. Neurosci. 16 (8): 2488–94.
  • Perin MS (1996). Mirror image motifs mediate the interaction of the COOH terminus of multiple synaptotagmins with the neurexins and calmodulin. Biochemistry 35 (43): 13808–13816.
  • Nguyen T, Südhof TC (1997). Binding properties of neuroligin 1 and neurexin 1beta reveal function as heterophilic cell adhesion molecules. J. Biol. Chem. 272 (41): 26032–26039.
  • Nagase T (1998). Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. DNA Res. 5 (1): 31–39.
  • Missler M, Hammer RE, Südhof TC (1999). Neurexophilin binding to alpha-neurexins. A single LNS domain functions as an independently folding ligand-binding unit. J. Biol. Chem. 273 (52): 34716–34723.
  • Kleiderlein JJ (1999). CCG repeats in cDNAs from human brain. Hum. Genet. 103 (6): 666–673.
  • Biederer T, Südhof TC (2001). Mints as adaptors. Direct binding to neurexins and recruitment of munc18. J. Biol. Chem. 275 (51): 39803–39806.
  • Koroll M, Rathjen FG, Volkmer H (2001). The neural cell recognition molecule neurofascin interacts with syntenin-1 but not with syntenin-2, both of which reveal self-associating activity. J. Biol. Chem. 276 (14): 10646–10654.
  • Fukuda M, Mikoshiba K (2001). Characterization of KIAA1427 protein as an atypical synaptotagmin (Syt XIII). Biochem. J. 354 (Pt 2): 249–57.
  • Fukuda M, Mikoshiba K (2001). Synaptotagmin-like protein 1-3: a novel family of C-terminal-type tandem C2 proteins. Biochem. Biophys. Res. Commun. 281 (5): 1226–1233.
  • Rowen L (2002). Analysis of the human neurexin genes: alternative splicing and the generation of protein diversity. Genomics 79 (4): 587–597.
  • Tabuchi K, Südhof TC (2002). Structure and evolution of neurexin genes: insight into the mechanism of alternative splicing. Genomics 79 (6): 849–859.
  • Nakayama M, Kikuno R, Ohara O (2003). Protein-protein interactions between large proteins: two-hybrid screening using a functionally classified library composed of long cDNAs. Genome Res. 12 (11): 1773–1784.

Template:PDB Gallery


This page uses Creative Commons Licensed content from Wikipedia (view authors).

Ad blocker interference detected!

Wikia is a free-to-use site that makes money from advertising. We have a modified experience for viewers using ad blockers

Wikia is not accessible if you’ve made further modifications. Remove the custom ad blocker rule(s) and the page will load as expected.