Synaptic arrangement of the neuroligin/beta-neurexin complex revealed by X-ray and neutron scattering

Comoletti, David, Grishaev, Alexander, Whitten, Andrew E., Tsignelny, Igor, Taylor, Palmer and Trewhella, Jill (2007) Synaptic arrangement of the neuroligin/beta-neurexin complex revealed by X-ray and neutron scattering. Structure, 15 6: 693-705. doi:10.1016/j.str.2007.04.010


Author Comoletti, David
Grishaev, Alexander
Whitten, Andrew E.
Tsignelny, Igor
Taylor, Palmer
Trewhella, Jill
Title Synaptic arrangement of the neuroligin/beta-neurexin complex revealed by X-ray and neutron scattering
Formatted title
Synaptic arrangement of the neuroligin/β-neurexin complex revealed by X-ray and neutron scattering
Journal name Structure   Check publisher's open access policy
ISSN 0969-2126
1878-4186
Publication date 2007-06-13
Sub-type Article (original research)
DOI 10.1016/j.str.2007.04.010
Volume 15
Issue 6
Start page 693
End page 705
Total pages 13
Place of publication Cambridge, Mass., U. S. A.
Publisher Cell Press
Language eng
Subject 0601 Biochemistry and Cell Biology
Formatted abstract
Neuroligins are postsynaptic cell-adhesion proteins that associate with their presynaptic partners, the neurexins. Using small-angle X-ray scattering, we determined the shapes of the extracellular region of several neuroligin isoforms in solution. We conclude that the neuroligins dimerize via the characteristic four-helix bundle observed in cholinesterases, and that the connecting sequence between the globular lobes of the dimer and the cell membrane is elongated, projecting away from the dimer interface. X-ray scattering and neutron contrast variation data show that two neurexin monomers, separated by 107 Å, bind at symmetric locations on opposite sides of the long axis of the neuroligin dimer. Using these data, we developed structural models that delineate the spatial arrangements of different neuroligin domains and their partnering molecules. As mutations of neurexin and neuroligin genes appear to be linked to autism, these models provide a structural framework for understanding altered recognition by these proteins in neurodevelopmental disorders.
©2007 Elsevier Ltd All rights reserved
Keyword Neuroligins
Neurodevelopmental disorders
Molneuro
Q-Index Code C1

Document type: Journal Article
Sub-type: Article (original research)
Collections: Excellence in Research Australia (ERA) - Collection
Institute for Molecular Bioscience - Publications
 
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Created: Fri, 19 Feb 2010, 12:14:10 EST by Sue Green on behalf of Institute for Molecular Bioscience