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Cover Picture: An Indole‐Binding Site is a Major Determinant of the Ligand Specificity of the GABA Type A Receptor‐Associated Protein GABARAP (ChemBioChem 11/2008)
Author(s) -
Thielmann Yvonne,
Mohrlüder Jeannine,
Koenig Bernd W.,
Stangler Thomas,
Hartmann Rudolf,
Becker Karin,
Höltje HansDieter,
Willbold Dieter
Publication year - 2008
Publication title -
chembiochem
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.200890040
Subject(s) - indole test , chemistry , tryptophan , ligand (biochemistry) , binding site , stereochemistry , nuclear magnetic resonance spectroscopy , titration , crystallography , receptor , amino acid , biochemistry , organic chemistry
The cover picture shows the NMR structure of the GABA A receptor associated protein (GABARAP) in a ribbon and surface representation with two bound tryptophans located in hydrophobic pockets on the surface of GABARAP. NMR spectroscopy allowed the mapping of the indole binding sites onto the surface of the protein and provided a quantitative estimate of the binding affinity. A subset of amide 1 H– 15 N correlation peaks of GABARAP in the two‐dimensional NMR spectrum show gradual positional shifts upon titration with tryptophan and other indole derivatives. This behavior is indicative of rapid ligand exchange on and off the binding site. Biological relevance of the indole binding sites for various GABARAP ligand interactions is indicated by the presence of conserved tryptophan residues in GABARAP ligands. Further details can be found in the article by D. Willbold, B. W. Koenig et al. on p. 1767 ff.