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

Kathleen Wood; Aviv Paz; Klaas Dijkstra; Ruud M. Scheek; Renee Otten; Israel Silman; Joel Sussman; Frans A. A. Mulder

doi:10.1007/s12104-011-9315-4

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

Kathleen Wood, Aviv Paz, Klaas Dijkstra, Ruud M. Scheek, Renee Otten, Israel Silman, Joel Sussman, Frans A. A. Mulder

Research output: Contribution to journal › Article › peer-review

6 Citations (Scopus)

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.

Original language	English
Pages (from-to)	15-18
Number of pages	4
Journal	Biomolecular NMR Assignments
Volume	6
Issue number	1
DOIs	https://doi.org/10.1007/s12104-011-9315-4
Publication status	Published - Apr 2012

All Science Journal Classification (ASJC) codes

Structural Biology
Biochemistry

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

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.",

author = "Kathleen Wood and Aviv Paz and Klaas Dijkstra and Scheek, {Ruud M.} and Renee Otten and Israel Silman and Joel Sussman and Mulder, {Frans A. A.}",

year = "2012",

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AU - Wood, Kathleen

AU - Paz, Aviv

AU - Dijkstra, Klaas

AU - Scheek, Ruud M.

AU - Otten, Renee

AU - Silman, Israel

AU - Sussman, Joel

AU - Mulder, Frans A. A.

PY - 2012/4

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N2 - 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.

AB - 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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U2 - 10.1007/s12104-011-9315-4

DO - 10.1007/s12104-011-9315-4

M3 - Article

SN - 1874-2718

VL - 6

SP - 15

EP - 18

JO - Biomolecular NMR Assignments

JF - Biomolecular NMR Assignments

IS - 1

ER -

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

Abstract

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