Journal Article

PreJuSER-7139

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Structural characterization of GABARAP-ligand interactions

Thielmann, Y.FZJ* ; Weiergräber, O. H.FZJ* ; Mohrlüder, J.FZJ* ; Willbold, D.FZJ*

2009
Royal Society of Chemistry Cambridge

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Please use a persistent id in citations: doi:10.1039/b900425d

Abstract: The GABA(A) receptor-associated protein (GABARAP) plays an important role in intracellular trafficking of several proteins. It undergoes a C-terminal lipidation process that enables anchoring in the cytosolic leaflet of cellular membranes. While the three-dimensional structure of GABARAP itself has been determined, structural investigation of complexes with its interaction partners has just commenced. Studies with indole derivatives revealed that GABARAP features two hydrophobic binding sites (hp1 and hp2). These also play an essential role in complex formation with the native ligand calreticulin. Furthermore, a model of hexameric N-ethylmaleimide-sensitive factor (NSF) suggests that binding of GABARAP to this molecular machine may involve a similar site. Since hp1 and hp2 are highly conserved throughout the GABARAP family, the relevance of the structural data presented here is likely to extend to GABARAP homologues.

Keyword(s): Amino Acid Sequence (MeSH) ; Animals (MeSH) ; Calreticulin: chemistry (MeSH) ; Calreticulin: metabolism (MeSH) ; Clathrin Heavy Chains: chemistry (MeSH) ; Clathrin Heavy Chains: metabolism (MeSH) ; Humans (MeSH) ; Ligands (MeSH) ; Models, Molecular (MeSH) ; Protein Binding (MeSH) ; Protein Structure, Tertiary (MeSH) ; Receptors, GABA-A: chemistry (MeSH) ; Receptors, GABA-A: metabolism (MeSH) ; Calreticulin ; Ligands ; Receptors, GABA-A ; Clathrin Heavy Chains ; J

Note: O.H.W. is grateful to Georg Buldt for continuous generous support. Moreover, assistance by the beamline staff at ESRF (Grenoble, France) is acknowledged. This study was supported by a research grant from the Deutsche Forschungsgemeinschaft to D. W. (Wi1472/5).

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Contributing Institute(s):

1. Strukturbiochemie (ISB-3)
2. Molekulare Biophysik (ISB-2)
3. Jülich Aachen Research Alliance - High-Performance Computing (JARA-HPC)

Research Program(s):

1. Funktion und Dysfunktion des Nervensystems (P33)
2. Programm Biosoft (N03)

Appears in the scientific report 2009

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