Cryo-EM advances in GPCR structure determination

G-protein-coupled receptors (GPCRs) constitute a prominent superfamily in humans, and are categorized into six classes (A through F) that play indispensable roles in cellular communication and therapeutics. Nonetheless, their structural comprehension has been limited by challenges in high-resolution...

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Veröffentlicht in:Journal of biochemistry (Tokyo) Jg. 176; H. 1; S. 1
Hauptverfasser: Shihoya, Wataru, Iwama, Aika, Sano, Fumiya K, Nureki, Osamu
Format: Journal Article
Sprache:Englisch
Veröffentlicht: England 01.07.2024
Schlagworte:
Cryo-EM
Structural biology
G-protein-coupled receptor
ISSN:1756-2651, 1756-2651
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Zusammenfassung:G-protein-coupled receptors (GPCRs) constitute a prominent superfamily in humans, and are categorized into six classes (A through F) that play indispensable roles in cellular communication and therapeutics. Nonetheless, their structural comprehension has been limited by challenges in high-resolution data acquisition. This review highlights the transformative impact of cryogenic electron microscopy (cryo-EM) in the structural determinations of GPCR-G-protein complexes. Specific technologies such as nanobodies and mini-G-proteins stabilize complexes and facilitate structural determination. We discuss the structural alterations upon receptor activation in different GPCR classes, revealing their diverse mechanisms. These cryo-EM structures provide a robust foundation for comprehending GPCR function and pave the way for future breakthroughs in drug discovery and therapeutic targeting.
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ISSN:1756-2651
1756-2651
DOI:10.1093/jb/mvae029