3D32
Complex of GABA(A) receptor-associated protein (GABARAP) with a synthetic peptide
Summary for 3D32
Entry DOI | 10.2210/pdb3d32/pdb |
Descriptor | Gamma-aminobutyric acid receptor-associated protein, K1 peptide, SODIUM ION, ... (5 entities in total) |
Functional Keywords | alpha-beta, beta-grasp fold, cytoskeleton, golgi apparatus, membrane, microtubule, transport, transport protein |
Biological source | Homo sapiens (Human) More |
Total number of polymer chains | 4 |
Total formula weight | 31456.17 |
Authors | Weiergraeber, O.H.,Stangler, T.,Willbold, D. (deposition date: 2008-05-09, release date: 2008-08-05, Last modification date: 2023-08-30) |
Primary citation | Weiergraber, O.H.,Stangler, T.,Thielmann, Y.,Mohrluder, J.,Wiesehan, K.,Willbold, D. Ligand Binding Mode of GABA(A) Receptor-Associated Protein. J.Mol.Biol., 381:1320-1331, 2008 Cited by PubMed 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. PubMed: 18638487DOI: 10.1016/j.jmb.2008.06.086 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.3 Å) |
Structure validation
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