5JTB
Crystal structure of the chimeric protein of A2aAR-BRIL with bound iodide ions
Summary for 5JTB
Entry DOI | 10.2210/pdb5jtb/pdb |
Related | 4EIY |
Descriptor | Adenosine receptor A2a,Soluble cytochrome b562,Adenosine receptor A2a, 4-{2-[(7-amino-2-furan-2-yl[1,2,4]triazolo[1,5-a][1,3,5]triazin-5-yl)amino]ethyl}phenol, CHOLESTEROL, ... (9 entities in total) |
Functional Keywords | membrane protein, iodide |
Biological source | Homo sapiens (Human) More |
Cellular location | Cell membrane; Multi-pass membrane protein: P29274 |
Total number of polymer chains | 1 |
Total formula weight | 56070.87 |
Authors | Melnikov, I.,Polovinkin, V.,Shevtsov, M.,Borshchevskiy, V.,Cherezov, V.,Popov, A.,Gordeliy, V. (deposition date: 2016-05-09, release date: 2017-05-31, Last modification date: 2024-11-13) |
Primary citation | Melnikov, I.,Polovinkin, V.,Kovalev, K.,Gushchin, I.,Shevtsov, M.,Shevchenko, V.,Mishin, A.,Alekseev, A.,Rodriguez-Valera, F.,Borshchevskiy, V.,Cherezov, V.,Leonard, G.A.,Gordeliy, V.,Popov, A. Fast iodide-SAD phasing for high-throughput membrane protein structure determination. Sci Adv, 3:e1602952-e1602952, 2017 Cited by PubMed Abstract: We describe a fast, easy, and potentially universal method for the de novo solution of the crystal structures of membrane proteins via iodide-single-wavelength anomalous diffraction (I-SAD). The potential universality of the method is based on a common feature of membrane proteins-the availability at the hydrophobic-hydrophilic interface of positively charged amino acid residues with which iodide strongly interacts. We demonstrate the solution using I-SAD of four crystal structures representing different classes of membrane proteins, including a human G protein-coupled receptor (GPCR), and we show that I-SAD can be applied using data collection strategies based on either standard or serial x-ray crystallography techniques. PubMed: 28508075DOI: 10.1126/sciadv.1602952 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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