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

Biomol NMR Assign. 2012 Apr;6(1):15-8. doi: 10.1007/s12104-011-9315-4. Epub 2011 Jun 7.

Authors

Kathleen Wood¹, Aviv Paz, Klaas Dijkstra, Ruud M Scheek, Renee Otten, Israel Silman, Joel L Sussman, Frans A A Mulder

Affiliation

¹ Department of Biophysical Chemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 7, 9747 AG Groningen, The Netherlands.

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 (1)H, (13)C and (15)N resonance assignments for the cytoplasmic domain of human neuroligin 3.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Amino Acid Sequence
Cell Adhesion Molecules, Neuronal / chemistry*
Cell Adhesion Molecules, Neuronal / metabolism
Cytoplasm / metabolism*
Humans
Membrane Proteins / chemistry*
Membrane Proteins / metabolism
Molecular Sequence Data
Nerve Tissue Proteins / chemistry*
Nerve Tissue Proteins / metabolism
Nuclear Magnetic Resonance, Biomolecular*
Protein Structure, Tertiary

Substances

Cell Adhesion Molecules, Neuronal
Membrane Proteins
Nerve Tissue Proteins
neuroligin 3