Synaptic arrangement of the neuroligin/β-neurexin complex revealed by x-ray and neutron scattering

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dc.contributor.authorComoletti, Den_AU
dc.contributor.authorGrishaev, Aen_AU
dc.contributor.authorWhitten, AEen_AU
dc.contributor.authorTsignelny, Ien_AU
dc.contributor.authorTaylor, Pen_AU
dc.contributor.authorTrewhella, Jen_AU
dc.date.accessioned2008-04-23T02:09:45Zen_AU
dc.date.accessioned2010-04-30T05:01:38Zen_AU
dc.date.available2008-04-23T02:09:45Zen_AU
dc.date.available2010-04-30T05:01:38Zen_AU
dc.date.issued2007-06en_AU
dc.date.statistics2007-06en_AU
dc.description.abstractNeuroligins 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 A, 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, Cell Pressen_AU
dc.identifier.citationComoletti, D., Grishaev, A., Whitten, A. E., Tsigelny, I., Taylor, P., & Trewhella, J. (2007). Synaptic arrangement of the neuroligin/β-neurexin complex revealed by x-ray and neutron scattering. Structure, 15(6), 693-705. doi:10.1016/j.str.2007.04.010en_AU
dc.identifier.govdoc1095en_AU
dc.identifier.issn0969-2126en_AU
dc.identifier.issue6en_AU
dc.identifier.journaltitleStructureen_AU
dc.identifier.pagination693-705en_AU
dc.identifier.urihttp://dx.doi.org/10.1016/j.str.2007.04.010en_AU
dc.identifier.urihttp://apo.ansto.gov.au/dspace/handle/10238/1106en_AU
dc.identifier.volume15en_AU
dc.language.isoenen_AU
dc.publisherElsevier (Cell Press)en_AU
dc.subjectNeutronsen_AU
dc.subjectProteinsen_AU
dc.subjectSmall angle scatteringen_AU
dc.subjectCholinesteraseen_AU
dc.subjectCell membranesen_AU
dc.subjectStructural modelsen_AU
dc.titleSynaptic arrangement of the neuroligin/β-neurexin complex revealed by x-ray and neutron scatteringen_AU
dc.typeJournal Articleen_AU
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