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Ligand binding mode of GABA(A) receptor-associated protein

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2008
Elsevier Amsterdam [u.a.]

Journal of molecular biology 381, 1320 - 1331 () [10.1016/j.jmb.2008.06.086]

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Abstract: 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.

Keyword(s): Adaptor Proteins, Signal Transducing: chemistry (MeSH) ; Adaptor Proteins, Signal Transducing: metabolism (MeSH) ; Humans (MeSH) ; Kinetics (MeSH) ; Ligands (MeSH) ; Magnetic Resonance Spectroscopy (MeSH) ; Microtubule-Associated Proteins: chemistry (MeSH) ; Microtubule-Associated Proteins: metabolism (MeSH) ; Models, Molecular (MeSH) ; Peptides: metabolism (MeSH) ; Protein Binding (MeSH) ; Protein Structure, Secondary (MeSH) ; Surface Plasmon Resonance (MeSH) ; Adaptor Proteins, Signal Transducing ; GABARAP protein, human ; Ligands ; Microtubule-Associated Proteins ; Peptides ; J ; GABARAP (auto) ; GABA(A) receptor (auto) ; synthetic peptide (auto) ; phage display (auto) ; X-ray crystallography (auto)


Note: 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).

Contributing Institute(s):
  1. Molekulare Biophysik (INB-2)
Research Program(s):
  1. Funktion und Dysfunktion des Nervensystems (P33)

Appears in the scientific report 2008
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ICS > ICS-6
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 Record created 2012-11-13, last modified 2020-04-02



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