3QCW

Structure of neurexin 1 alpha (domains LNS1-LNS6), no splice inserts

Summary for 3QCW

• Entry DOI: 10.2210/pdb3qcw/pdb
• Descriptor: Neurexin-1-alpha, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose (2 entities in total)
• Functional Keywords: synaptic adhesion molecule, cell adhesion
• Biological source: Bos taurus (bovine); More
• Cellular location: Cell membrane ; Single-pass type I membrane protein : Q28146
• Total number of polymer chains: 2
• Total formula weight: 275798.08

Authors

Rudenko, G. (deposition date: 2011-01-17, release date: 2011-06-15, Last modification date: 2024-11-06)

Primary citation

Chen, F.,Venugopal, V.,Murray, B.,Rudenko, G.
The Structure of Neurexin 1 alpha Reveals Features Promoting a Role as Synaptic Organizer
Structure, 19:779-789, 2011

PubMed Abstract: 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 Å. 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 Å 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.

PubMed: 21620716
DOI: 10.1016/j.str.2011.03.012

Experimental method

X-RAY DIFFRACTION (2.65 Å)