Description: Structural characterization of GABARAP-ligand interactions

This title appears in the Scientific Report : 2009

Structural characterization of GABARAP-ligand interactions

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...

Personal Name(s):	Thielmann, Y.
	Weiergräber, O.H. / Mohrlüder, J. / Willbold, D.
Contributing Institute:	Strukturbiochemie; ISB-3 JARA - HPC; JARA-HPC Molekulare Biophysik; ISB-2
Published in:	Molecular BioSystems, 5 (2009) S. 575 - 579
Imprint:	Cambridge Royal Society of Chemistry 2009
Physical Description:	575 - 579
PubMed ID:	19462014
DOI:	10.1039/b900425d
Document Type:	Journal Article
Research Program:	Programm Biosoft Funktion und Dysfunktion des Nervensystems
Series Title:	Molecular BioSystems 5
Subject (ZB):	Amino Acid Sequence Animals Calreticulin: chemistry Calreticulin: metabolism Clathrin Heavy Chains: chemistry Clathrin Heavy Chains: metabolism Humans Ligands Models, Molecular Protein Binding Protein Structure, Tertiary Receptors, GABA-A: chemistry Receptors, GABA-A: metabolism Calreticulin Receptors, GABA-A Clathrin Heavy Chains J
	Publikationsportal JuSER

Please use the identifier: http://dx.doi.org/10.1039/b900425d in citations.

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.