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 (1)H, (13)C and (15)N resonance assignments for the cytoplasmic domain of human neuroligin 3.
authors.affiliation: Department of Biophysical Chemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 7, 9747 AG Groningen, The Netherlands.
authors.forename: Kathleen
authors.initials: K
authors.lastname: Wood
authors.forename: Aviv
authors.initials: A
authors.lastname: Paz
authors.forename: Klaas
authors.initials: K
authors.lastname: Dijkstra
authors.forename: Ruud M
authors.initials: RM
authors.lastname: Scheek
authors.forename: Renee
authors.initials: R
authors.lastname: Otten
authors.forename: Israel
authors.initials: I
authors.lastname: Silman
authors.forename: Joel L
authors.initials: JL
authors.lastname: Sussman
authors.forename: Frans A A
authors.initials: FA
authors.lastname: Mulder
mesh_terms: D000595:Amino Acid Sequence; D015816:Cell Adhesion Molecules, Neuronal / Q000737:chemistry* / Q000378:metabolism; D003593:Cytoplasm / Q000378:metabolism*; D006801:Humans; D008565:Membrane Proteins / Q000737:chemistry* / Q000378:metabolism; D008969:Molecular Sequence Data; D009419:Nerve Tissue Proteins / Q000737:chemistry* / Q000378:metabolism; D019906:Nuclear Magnetic Resonance, Biomolecular; D017434:Protein Structure, Tertiary
chemical_list: D015816:Cell Adhesion Molecules, Neuronal; D008565:Membrane Proteins; D009419:Nerve Tissue Proteins; C098004:neuroligin 3