TY  - JOUR
AU  - Thielmann, Y.
AU  - Weiergräber, O.H.
AU  - Mohrlüder, J.
AU  - Willbold, D.
TI  - Structural characterization of GABARAP-ligand interactions
JO  - Molecular BioSystems
VL  - 5
SN  - 1742-206X
CY  - Cambridge
PB  - Royal Society of Chemistry
M1  - PreJuSER-7139
SP  - 575 - 579
PY  - 2009
N1  - 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).
AB  - 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.
KW  - Amino Acid Sequence
KW  - Animals
KW  - Calreticulin: chemistry
KW  - Calreticulin: metabolism
KW  - Clathrin Heavy Chains: chemistry
KW  - Clathrin Heavy Chains: metabolism
KW  - Humans
KW  - Ligands
KW  - Models, Molecular
KW  - Protein Binding
KW  - Protein Structure, Tertiary
KW  - Receptors, GABA-A: chemistry
KW  - Receptors, GABA-A: metabolism
KW  - Calreticulin (NLM Chemicals)
KW  - Ligands (NLM Chemicals)
KW  - Receptors, GABA-A (NLM Chemicals)
KW  - Clathrin Heavy Chains (NLM Chemicals)
KW  - J (WoSType)
LB  - PUB:(DE-HGF)16
C6  - pmid:19462014
UR  - <Go to ISI:>//WOS:000266269500002
DO  - DOI:10.1039/b900425d
UR  - https://juser.fz-juelich.de/record/7139
ER  -