Macromolecular architecture of extracellular domain of αNRXN1: domain organization, flexibility, and insights into trans-synaptic disposition.

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dc.contributor.authorComoletti, Den_AU
dc.contributor.authorMiller, MTen_AU
dc.contributor.authorJeffries, CMen_AU
dc.contributor.authorWilson, Jen_AU
dc.contributor.authorDemeler, Ben_AU
dc.contributor.authorTaylor, Pen_AU
dc.contributor.authorTrewhella, Jen_AU
dc.contributor.authorNakagawa, Ten_AU
dc.date.accessioned2010-09-09T06:56:25Zen_AU
dc.date.available2010-09-09T06:56:25Zen_AU
dc.date.issued2010-08-11en_AU
dc.date.statistics2010-08-11en_AU
dc.description.abstractNeurexins are multidomain synaptic cell-adhesion proteins that associate with multiple partnering proteins. Genetic evidence indicates that neurexins may contribute to autism, schizophrenia, and nicotine dependence. Using analytical ultracentrifugation, single-particle electron microscopy, and solution X-ray scattering, we obtained a three-dimensional structural model of the entire extracellular domain of neurexin-1α. This protein adopts a dimensionally asymmetric conformation that is monomeric in solution, with a maximum dimension of ~ 170 Å. The extracellular domain of α-neurexin maintains a characteristic “Y” shape, whereby LNS domains 1–4 form an extended base of the “Y” and LNS5-6 the shorter arms. Moreover, two major regions of flexibility are present: one between EGF1 and LNS2, corresponding to splice site 1, another between LNS5 and 6. We thus provide the first structural insights into the architecture of the extracellular region of neurexin-1α, show how the protein may fit in the synaptic cleft, and how partnering proteins could bind simultaneously. © 2010, Cell Pressen_AU
dc.identifier.citationComoletti, D., Miller, M. T., Jeffries, C. M., Wilson, J., Demeler, B., Taylor, P., Trewhella, J., & Nakagawa, T. (2010). Macromolecular architecture of extracellular domain of αNRXN1: domain organization, flexibility, and insights into trans-synaptic disposition. Structure, 18(8), 1044-1053. doi:10.1016/j.str.2010.06.005en_AU
dc.identifier.govdoc2642en_AU
dc.identifier.issn0969-2126en_AU
dc.identifier.issue8en_AU
dc.identifier.journaltitleStructureen_AU
dc.identifier.pagination1044-1053en_AU
dc.identifier.urihttp://dx.doi.org/10.1016/j.str.2010.06.005en_AU
dc.identifier.urihttp://apo.ansto.gov.au/dspace/handle/10238/2481en_AU
dc.identifier.volume18en_AU
dc.language.isoenen_AU
dc.publisherElsevier (Cell Press)en_AU
dc.subjectCrystal structureen_AU
dc.subjectMental disordersen_AU
dc.subjectLigandsen_AU
dc.subjectAdhesionen_AU
dc.subjectProteinsen_AU
dc.subjectUltracentrifugationen_AU
dc.titleMacromolecular architecture of extracellular domain of αNRXN1: domain organization, flexibility, and insights into trans-synaptic disposition.en_AU
dc.typeJournal Articleen_AU
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