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 L. 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 L. Sussman
, Frans A.A. Mulder

Department of Structural Biology

University of Groningen
Australian Nuclear Science and Technology Organisation
Weizmann Institute of Science

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

6 Scopus citations

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
State	Published - Apr 2012

Keywords

Cholinesterase-like adhesion molecule
Intrinsically disordered protein
Neural cell adhesion
PDZ-binding domain

Access to Document

10.1007/s12104-011-9315-4

Cite this

@article{84c8adc5869345acb6db8c44008ed36c,

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.",

keywords = "Cholinesterase-like adhesion molecule, Intrinsically disordered protein, Neural cell adhesion, PDZ-binding domain",

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

year = "2012",

month = apr,

doi = "10.1007/s12104-011-9315-4",

language = "English",

volume = "6",

pages = "15--18",

journal = "Biomolecular NMR Assignments",

issn = "1874-2718",

publisher = "Springer Science and Business Media B.V.",

number = "1",

}

TY - JOUR

T1 - Backbone and side chain NMR assignments for the intrinsically disordered cytoplasmic domain of human neuroligin-3

AU - Wood, Kathleen

AU - Paz, Aviv

AU - Dijkstra, Klaas

AU - Scheek, Ruud M.

AU - Otten, Renee

AU - Silman, Israel

AU - Sussman, Joel L.

AU - Mulder, Frans A.A.

PY - 2012/4

Y1 - 2012/4

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.

KW - Cholinesterase-like adhesion molecule

KW - Intrinsically disordered protein

KW - Neural cell adhesion

KW - PDZ-binding domain

UR - https://www.scopus.com/pages/publications/84858278489

U2 - 10.1007/s12104-011-9315-4

DO - 10.1007/s12104-011-9315-4

M3 - Article

C2 - 21647611

AN - SCOPUS:84858278489

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

Keywords

Access to Document

Other files and links

Fingerprint

Cite this