1GNU
GABA(A) receptor associated protein GABARAP
1GNU の概要
| エントリーDOI | 10.2210/pdb1gnu/pdb |
| 分子名称 | GABARAP, NICKEL (II) ION (3 entities in total) |
| 機能のキーワード | transport, ubiquitin-like, receptor |
| 由来する生物種 | HOMO SAPIENS (HUMAN) |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 14000.74 |
| 構造登録者 | Knight, D.,Harris, R.,Moss, S.,Driscoll, P.C.,Keep, N.H. (登録日: 2001-10-09, 公開日: 2001-12-03, 最終更新日: 2023-12-13) |
| 主引用文献 | Knight, D.,Harris, R.,Mcalister, M.,Phelan, J.,Geddes, S.,Moss, S.,Driscoll, P.C.,Keep, N.H. The X-Ray Crystal Structure and Putative Ligand-Derived Peptide Binding Properties of Gamma-Aminobutyric Acid Receptor Type a Receptor-Associated Protein J.Biol.Chem., 277:5556-, 2002 Cited by PubMed Abstract: The gamma-aminobutyric acid receptor type A (GABA(A)) receptor-associated protein (GABARAP) has been reported to mediate the interaction between the GABA(A) receptor and microtubules. We present the three-dimensional structure of GABARAP obtained by x-ray diffraction at 1.75 A resolution. The structure was determined by molecular replacement using the structure of the homologous protein GATE-16. NMR spectroscopy of isotope-labeled GABARAP showed the structure in solution to be compatible with the overall fold but showed evidence of conformation heterogeneity that is not apparent in the crystal structure. We assessed the binding of GABARAP to peptides derived from reported binding partner proteins, including the M3-M4 loop of the gamma2 subunit of the GABA(A) receptor and the acidic carboxyl-terminal tails of human alpha- and beta-tubulin. There is a small area of concentrated positive charge on one surface of GABARAP, which we found interacts weakly with all peptides tested, but we found no evidence for specific binding to the proposed physiological target peptides. These results are compatible with a more general role in membrane targeting and transportation for the GABARAP family of proteins. PubMed: 11729197DOI: 10.1074/JBC.M109753200 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.75 Å) |
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