Skip to main content
  • Poster presentation
  • Open access
  • Published:

Identification of small aromatic ligands to GABA-A receptor associated protein GABARAP

Type-A receptors for the neurotransmitter GABA (gamma-aminobutyric acid) are ligand-gated chloride channels that mediate inhibitory neuro-transmission. The 14 kDa GABA-A receptor associated protein GABARAP interacts with the gamma2 subunit of GABA-A receptor and modulates channel kinetics and promotes channel clustering. GABARAP is involved in receptor trafficking and targeting to GABAergic synapses.

With Phage Display methods we identified peptides with micromolar affinity for GABARAP. Although exhibiting great sequence diversity, the most prominent common feature of the selected peptides was a tryptophan residue occurring in all peptides. This lead us to further investigate the role of this tryptophan residue in GABARAP-ligand interactions.

We used saturation transfer difference NMR (STDNMR) in order to identify tryptophan-derived small aromatic molecules which interact with GABARAP. Chemical shift perturbation and J-surface analysis allowed for mapping of the indole moiety's binding site to GABARAP.

Author information

Authors and Affiliations


Rights and permissions

Open Access This article is published under license to BioMed Central Ltd. This is an Open Access article is distributed under the terms of the Creative Commons Attribution 2.0 International License (, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Reprints and permissions

About this article

Cite this article

Stangler, T., Mohrlüder, J., Hoffmann, Y. et al. Identification of small aromatic ligands to GABA-A receptor associated protein GABARAP. BMC Neurosci 8 (Suppl 1), P20 (2007).

Download citation

  • Published:

  • DOI: