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Backbone and side chain NMR assignments for the intrinsically disordered cytoplasmic domain of human neuroligin-3 |
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| Authors: | Kathleen Wood Aviv Paz Klaas Dijkstra Ruud M Scheek Renee Otten Israel Silman Joel L Sussman Frans A A Mulder |
| Institution: | (1) Department of Biophysical Chemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 7, 9747 AG Groningen, The Netherlands;(2) Department of Neurobiology, Weizmann Institute of Science, Rehovot, Israel;(3) Department of Structural Biology, Weizmann Institute of Science, Rehovot, Israel;(4) Present address: Bragg Institute, Australian Nuclear Science and Technology Organisation, Menai, NSW, Australia;(5) Present address: Department of Physiology, David Geffen School of Medicine, University of California, Los Angeles, CA 90095-1751, USA; |
| Abstract: | Neuroligins act as heterophilic adhesion molecules at neuronal synapses. Their cytoplasmic domains interact with synaptic scaffolding proteins, and have been shown to be intrinsically disordered. Here we report the backbone and side chain 1H, 13C and 15N resonance assignments for the cytoplasmic domain of human neuroligin 3. |
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