Backbone and side chain NMR assignments for the intrinsically disordered cytoplasmic domain of human neuroligin-3

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 (1)H, (13)C and (15)N resonance assignments for the cytoplasm...

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Autores principales: Wood, Kathleen, Paz, Aviv, Dijkstra, Klaas, Scheek, Ruud M., Otten, Renee, Silman, Israel, Sussman, Joel L., Mulder, Frans A. A.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer Netherlands 2011
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3298649/
https://www.ncbi.nlm.nih.gov/pubmed/21647611
http://dx.doi.org/10.1007/s12104-011-9315-4
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author Wood, Kathleen
Paz, Aviv
Dijkstra, Klaas
Scheek, Ruud M.
Otten, Renee
Silman, Israel
Sussman, Joel L.
Mulder, Frans A. A.
author_facet Wood, Kathleen
Paz, Aviv
Dijkstra, Klaas
Scheek, Ruud M.
Otten, Renee
Silman, Israel
Sussman, Joel L.
Mulder, Frans A. A.
author_sort Wood, Kathleen
collection PubMed
description 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 (1)H, (13)C and (15)N resonance assignments for the cytoplasmic domain of human neuroligin 3.
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spelling pubmed-32986492012-03-21 Backbone and side chain NMR assignments for the intrinsically disordered cytoplasmic domain of human neuroligin-3 Wood, Kathleen Paz, Aviv Dijkstra, Klaas Scheek, Ruud M. Otten, Renee Silman, Israel Sussman, Joel L. Mulder, Frans A. A. Biomol NMR Assign Article 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 (1)H, (13)C and (15)N resonance assignments for the cytoplasmic domain of human neuroligin 3. Springer Netherlands 2011-06-07 2012 /pmc/articles/PMC3298649/ /pubmed/21647611 http://dx.doi.org/10.1007/s12104-011-9315-4 Text en © The Author(s) 2011 https://creativecommons.org/licenses/by-nc/4.0/ This article is distributed under the terms of the Creative Commons Attribution Noncommercial License which permits any noncommercial use, distribution, and reproduction in any medium, provided the original author(s) and source are credited.
spellingShingle Article
Wood, Kathleen
Paz, Aviv
Dijkstra, Klaas
Scheek, Ruud M.
Otten, Renee
Silman, Israel
Sussman, Joel L.
Mulder, Frans A. A.
Backbone and side chain NMR assignments for the intrinsically disordered cytoplasmic domain of human neuroligin-3
title Backbone and side chain NMR assignments for the intrinsically disordered cytoplasmic domain of human neuroligin-3
title_full Backbone and side chain NMR assignments for the intrinsically disordered cytoplasmic domain of human neuroligin-3
title_fullStr Backbone and side chain NMR assignments for the intrinsically disordered cytoplasmic domain of human neuroligin-3
title_full_unstemmed Backbone and side chain NMR assignments for the intrinsically disordered cytoplasmic domain of human neuroligin-3
title_short Backbone and side chain NMR assignments for the intrinsically disordered cytoplasmic domain of human neuroligin-3
title_sort backbone and side chain nmr assignments for the intrinsically disordered cytoplasmic domain of human neuroligin-3
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3298649/
https://www.ncbi.nlm.nih.gov/pubmed/21647611
http://dx.doi.org/10.1007/s12104-011-9315-4
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