کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
2029821 1070978 2010 10 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
The Macromolecular Architecture of Extracellular Domain of αNRXN1: Domain Organization, Flexibility, and Insights into Trans-Synaptic Disposition
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی زیست شیمی
پیش نمایش صفحه اول مقاله
The Macromolecular Architecture of Extracellular Domain of αNRXN1: Domain Organization, Flexibility, and Insights into Trans-Synaptic Disposition
چکیده انگلیسی

SummaryNeurexins 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.


► The extracellular domain of αNRXN1 is monomeric in solution
► αNRXN1 maintains a characteristic “Y” shape in solution
► Extensive flexibility is present between LNS1 and 2 and between LNS5 and 6
► A three-dimensional structural model of the αNRXN1 is presented and discussed

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: - Volume 18, Issue 8, 11 August 2010, Pages 1044–1053
نویسندگان
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