1C4R

THE STRUCTURE OF THE LIGAND-BINDING DOMAIN OF NEUREXIN 1BETA: REGULATION OF LNS DOMAIN FUNCTION BY ALTERNATIVE SPLICING

Summary for 1C4R

• Entry DOI: 10.2210/pdb1c4r/pdb
• Descriptor: NEUREXIN-I BETA (2 entities in total)
• Functional Keywords: lectin-like, neurobiology, cell-cell adhesion, cell-cell recognition, alternative splicing, membrane protein
• Biological source: Rattus norvegicus (Norway rat)
• Cellular location: Membrane; Single-pass type I membrane protein (Potential): Q63373
• Total number of polymer chains: 8
• Total formula weight: 157544.58

Authors

Rudenko, G.,Nguyen, T.,Chelliah, Y.,Sudhof, T.C.,Deisenhofer, J. (deposition date: 1999-09-28, release date: 2000-10-04, Last modification date: 2023-12-27)

Primary citation

Rudenko, G.,Nguyen, T.,Chelliah, Y.,Sudhof, T.C.,Deisenhofer, J.
The structure of the ligand-binding domain of neurexin Ibeta: regulation of LNS domain function by alternative splicing.
Cell(Cambridge,Mass.), 99:93-101, 1999

PubMed 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 Ibeta, a single LNS domain, reveals two seven-stranded beta 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.

PubMed: 10520997
DOI: 10.1016/S0092-8674(00)80065-3

Experimental method

X-RAY DIFFRACTION (2.6 Å)