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

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

Documents

DOI

  • Kathleen Wood
  • ,
  • Aviv Paz
  • ,
  • Klaas Dijkstra
  • ,
  • Ruud M Scheek
  • ,
  • Renee Otten
  • ,
  • Israel Silman
  • ,
  • Joel L Sussman
  • ,
  • Frans A.A. Mulder
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.
Original languageEnglish
JournalBiomolecular N M R Assignments
Volume6
Issue1
Pages (from-to)15-8
Number of pages4
ISSN1874-2718
DOIs
Publication statusPublished - 2012

    Research areas

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

See relations at Aarhus University Citationformats

Download statistics

No data available

ID: 50933676