3d32

Complex of GABA(A) receptor-associated protein (GABARAP) with a synthetic peptide

spinqualitylabelsall models 3d32, resolution 1.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3d32 is a 4 chain structure with sequence from Homo sapiens and Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.3Å Ligands: CL, NA, NH2 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function GBRAP_HUMAN May play a role in intracellular transport of GABA(A) receptors and its interaction with the cytoskeleton. Involved in apoptosis. Involved in autophagy (By similarity). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. Ligand binding mode of GABAA receptor-associated protein.,Weiergraber OH, Stangler T, Thielmann Y, Mohrluder J, Wiesehan K, Willbold D J Mol Biol. 2008 Sep 19;381(5):1320-31. Epub 2008 Jul 7. PMID:18638487 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also GABA receptor-associated protein 3D structures

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