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- W3203752479 abstract "G protein-coupled receptors (GPCRs) are the largest single family of cell surface receptors encoded by the human genome and they play pivotal roles in co-ordinating cellular systems throughout the human body, making them ideal drug targets. Structural biology has played a key role in defining how receptors are activated and signal through G proteins and β-arrestins. The application of structure-based drug design (SBDD) is now yielding novel compounds targeting GPCRs. There is thus significant interest from both academia and the pharmaceutical industry in the structural biology of GPCRs as currently only about one quarter of human non-odorant receptors have had their structure determined. Initially, all the structures were determined by X-ray crystallography, but recent advances in electron cryo-microscopy (cryo-EM) now make GPCRs tractable targets for single-particle cryo-EM with comparable resolution to X-ray crystallography. So far this year, 78% of the 99 GPCR structures deposited in the PDB (Jan-Jul 2021) were determined by cryo-EM. Cryo-EM has also opened up new possibilities in GPCR structural biology, such as determining structures of GPCRs embedded in a lipid nanodisc and multiple GPCR conformations from a single preparation. However, X-ray crystallography still has a number of advantages, particularly in the speed of determining many structures of the same receptor bound to different ligands, an essential prerequisite for effective SBDD. We will discuss the relative merits of cryo-EM and X-ray crystallography for the structure determination of GPCRs and the future potential of both techniques." @default.
- W3203752479 created "2021-10-11" @default.
- W3203752479 creator A5008339304 @default.
- W3203752479 creator A5089964906 @default.
- W3203752479 date "2021-09-28" @default.
- W3203752479 modified "2023-10-16" @default.
- W3203752479 title "Structure determination of GPCRs: cryo-EM compared with X-ray crystallography" @default.
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- W3203752479 doi "https://doi.org/10.1042/bst20210431" @default.
- W3203752479 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/8589417" @default.
- W3203752479 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/34581758" @default.
- W3203752479 hasPublicationYear "2021" @default.
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