The structure of neurexin 1α reveals features promoting a role as synaptic organizer

Fang Chen, Vandavasi Venugopal, Beverly Murray, Gabby Rudenko

Research output: Contribution to journalArticlepeer-review

61 Scopus citations


α-Neurexins are essential synaptic adhesion molecules implicated in autism spectrum disorder and schizophrenia. The α-neurexin extracellular domain consists of six LNS domains interspersed by three EGF-like repeats and interacts with many different proteins in the synaptic cleft. To understand how α-neurexins might function as synaptic organizers, we solved the structure of the neurexin 1α extracellular domain (n1α) to 2.65 . The L-shaped molecule can be divided into a flexible repeat I (LNS1-EGF-A-LNS2), a rigid horseshoe-shaped repeat II (LNS3-EGF-B-LNS4) with structural similarity to so-called reelin repeats, and an extended repeat III (LNS5-EGF-B-LNS6) with controlled flexibility. A 2.95 structure of n1α carrying splice insert SS#3 in LNS4 reveals that SS#3 protrudes as a loop and does not alter the rigid arrangement of repeat II. The global architecture imposed by conserved structural features enables α-neurexins to recruit and organize proteins in distinct and variable ways, influenced by splicing, thereby promoting synaptic function.

Original languageEnglish (US)
Pages (from-to)779-789
Number of pages11
Issue number6
StatePublished - Jun 8 2011
Externally publishedYes

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology


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