TY  - JOUR
AU  - Weiergräber, O. H.
AU  - Stangler, T.
AU  - Thielmann, Y.
AU  - Mohrlüder, J.
AU  - Wiesehan, K.
AU  - Willbold, D.
TI  - Ligand binding mode of GABA(A) receptor-associated protein
JO  - Journal of molecular biology
VL  - 381
SN  - 0022-2836
CY  - Amsterdam [u.a.]
PB  - Elsevier
M1  - PreJuSER-344
SP  - 1320 - 1331
PY  - 2008
N1  - The authors wish to thank Joachim Granzin for helpful discussion and Olga Dietz for excellent technical assistance. O.H.W. is grateful to Georg Buldt for continuous generous support. Moreover, assistance by the ESRF staff at beamline ID14-1 is acknowledged. This study was supported by a research grant from the Deutsche Forschungsgemeinschaft to D.W. (Wi1472/5).
AB  - The gamma-aminobutyric acid type A (GABA(A)) receptor-associated protein is a versatile adaptor protein playing an important role in intracellular vesicle trafficking, particularly in neuronal cells. We present the X-ray structure of the soluble form of human GABA(A) receptor-associated protein complexed with a high-affinity synthetic peptide at 1.3 A resolution. The data shed light on the probable binding modes of key interaction partners, including the GABA(A) receptor and the cysteine protease Atg4. The resulting models provide a structural background for further investigation of the unique biological properties of this protein.
KW  - Adaptor Proteins, Signal Transducing: chemistry
KW  - Adaptor Proteins, Signal Transducing: metabolism
KW  - Humans
KW  - Kinetics
KW  - Ligands
KW  - Magnetic Resonance Spectroscopy
KW  - Microtubule-Associated Proteins: chemistry
KW  - Microtubule-Associated Proteins: metabolism
KW  - Models, Molecular
KW  - Peptides: metabolism
KW  - Protein Binding
KW  - Protein Structure, Secondary
KW  - Surface Plasmon Resonance
KW  - Adaptor Proteins, Signal Transducing (NLM Chemicals)
KW  - GABARAP protein, human (NLM Chemicals)
KW  - Ligands (NLM Chemicals)
KW  - Microtubule-Associated Proteins (NLM Chemicals)
KW  - Peptides (NLM Chemicals)
KW  - J (WoSType)
LB  - PUB:(DE-HGF)16
C6  - pmid:18638487
UR  - <Go to ISI:>//WOS:000259169100019
DO  - DOI:10.1016/j.jmb.2008.06.086
UR  - https://juser.fz-juelich.de/record/344
ER  -