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Publication Abstract from PubMed

alpha-Neurexins are essential synaptic adhesion molecules implicated in autism spectrum disorder and schizophrenia. The alpha-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 alpha-neurexins might function as synaptic organizers, we solved the structure of the neurexin 1alpha extracellular domain (n1alpha) to 2.65 A. 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 A structure of n1alpha 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 alpha-neurexins to recruit and organize proteins in distinct and variable ways, influenced by splicing, thereby promoting synaptic function.

The structure of neurexin 1alpha reveals features promoting a role as synaptic organizer.,Chen F, Venugopal V, Murray B, Rudenko G Structure. 2011 Jun 8;19(6):779-89. Epub 2011 May 27. PMID:21620716^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.