The structure of the ligand-binding domain of neurexin Iβ: Regulation of LNS domain function by alternative splicing

Gabby Rudenko, Thai Nguyen, Yogarany Chelliah, Thomas C. Südhof, Johann Deisenhofer

Research output: Contribution to journalArticlepeer-review

111 Scopus citations

Abstract

Neurexins are expressed in hundreds of isoforms on the neuronal cell surface, where they may function as cell recognition molecules. Neurexins contain LNS domains, folding units found in many proteins like the G domain of laminin A, agrin, and slit. The crystal structure of neurexin Iβ, a single LNS domain, reveals two seven-stranded β sheets forming a jelly roll fold with unexpected structural similarity to lectins. The LNS domains of neurexin and agrin undergo alternative splicing that modulates their affinity for protein ligands in a neuron-specific manner. These splice sites are localized within loops at one edge of the jelly roll, suggesting a distinct protein interaction surface in LNS domains that is regulated by alternative splicing.

Original languageEnglish (US)
Pages (from-to)93-101
Number of pages9
JournalCell
Volume99
Issue number1
DOIs
StatePublished - Oct 1 1999
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

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