TY - JOUR
T1 - The structure of the ligand-binding domain of neurexin Iβ
T2 - Regulation of LNS domain function by alternative splicing
AU - Rudenko, Gabby
AU - Nguyen, Thai
AU - Chelliah, Yogarany
AU - Südhof, Thomas C.
AU - Deisenhofer, Johann
PY - 1999/10/1
Y1 - 1999/10/1
N2 - 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.
AB - 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.
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U2 - 10.1016/S0092-8674(00)80065-3
DO - 10.1016/S0092-8674(00)80065-3
M3 - Article
C2 - 10520997
AN - SCOPUS:0033215463
SN - 0092-8674
VL - 99
SP - 93
EP - 101
JO - Cell
JF - Cell
IS - 1
ER -