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5JTB

Crystal structure of the chimeric protein of A2aAR-BRIL with bound iodide ions

Summary for 5JTB
Entry DOI10.2210/pdb5jtb/pdb
Related4EIY
DescriptorAdenosine 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 Keywordsmembrane protein, iodide
Biological sourceHomo sapiens (Human)
More
Cellular locationCell membrane; Multi-pass membrane protein: P29274
Total number of polymer chains1
Total formula weight56070.87
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 citationMelnikov, 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: 28508075
DOI: 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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