Title of article :
Ligand Binding Mode of GABAA Receptor-Associated Protein
Author/Authors :
Oliver H. Weiergr?ber، نويسنده , , Thomas Stangler، نويسنده , , Yvonne Thielmann، نويسنده , , Jeannine Mohrlüder، نويسنده , , Katja Wiesehan، نويسنده , , Dieter Willbold، نويسنده ,
Issue Information :
روزنامه با شماره پیاپی سال 2008
Pages :
12
From page :
1320
To page :
1331
Abstract :
The γ-aminobutyric acid type A (GABAA) 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 GABAA receptor-associated protein complexed with a high-affinity synthetic peptide at 1.3 Å resolution. The data shed light on the probable binding modes of key interaction partners, including the GABAA receptor and the cysteine protease Atg4. The resulting models provide a structural background for further investigation of the unique biological properties of this protein.
Keywords :
GABARAP , GABAA receptor , phage display , synthetic peptide , X-ray crystallography
Journal title :
Journal of Molecular Biology
Serial Year :
2008
Journal title :
Journal of Molecular Biology
Record number :
1257368
Link To Document :
بازگشت