دورية أكاديمية
Cryo-EM advances in GPCR structure determination.
| العنوان: | Cryo-EM advances in GPCR structure determination. |
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| المؤلفون: | Shihoya W; Department of Biological Sciences, Graduate School of Science, The University of Tokyo, 7-3-1 Hongo, Bunkyo-Ku, Tokyo 113-0033, Japan., Iwama A; Department of Biological Sciences, Graduate School of Science, The University of Tokyo, 7-3-1 Hongo, Bunkyo-Ku, Tokyo 113-0033, Japan., Sano FK; Department of Biological Sciences, Graduate School of Science, The University of Tokyo, 7-3-1 Hongo, Bunkyo-Ku, Tokyo 113-0033, Japan., Nureki O; Department of Biological Sciences, Graduate School of Science, The University of Tokyo, 7-3-1 Hongo, Bunkyo-Ku, Tokyo 113-0033, Japan. |
| المصدر: | Journal of biochemistry [J Biochem] 2024 Jul 01; Vol. 176 (1), pp. 1-10. |
| نوع المنشور: | Journal Article; Review |
| اللغة: | English |
| بيانات الدورية: | Publisher: Oxford University Press Country of Publication: England NLM ID: 0376600 Publication Model: Print Cited Medium: Internet ISSN: 1756-2651 (Electronic) Linking ISSN: 0021924X NLM ISO Abbreviation: J Biochem Subsets: MEDLINE |
| أسماء مطبوعة: | Publication: Original Publication: Tokyo : Japanese Biochemical Society |
| مواضيع طبية MeSH: | Cryoelectron Microscopy*/methods , Receptors, G-Protein-Coupled*/metabolism , Receptors, G-Protein-Coupled*/chemistry, Humans ; Protein Conformation ; Animals ; Single-Domain Antibodies/chemistry ; Single-Domain Antibodies/metabolism ; Single-Domain Antibodies/immunology ; Models, Molecular |
| مستخلص: | G-protein-coupled receptors (GPCRs) constitute a prominent superfamily in humans and are categorized into six classes (A-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) on 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. This review highlights the robust foundation for comprehending GPCR function and pave the way for future breakthroughs in drug discovery and therapeutic targeting. (© The Author(s) 2024. Published by Oxford University Press on behalf of the Japanese Biochemical Society. All rights reserved.) |
| فهرسة مساهمة: | Keywords: G-protein-coupled receptor; cryo-EM; structural biology |
| المشرفين على المادة: | 0 (Receptors, G-Protein-Coupled) 0 (Single-Domain Antibodies) |
| تواريخ الأحداث: | Date Created: 20240318 Date Completed: 20240702 Latest Revision: 20240702 |
| رمز التحديث: | 20240703 |
| DOI: | 10.1093/jb/mvae029 |
| PMID: | 38498911 |
| قاعدة البيانات: | MEDLINE |
Full Text Finder | تدمد: | 1756-2651 |
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| DOI: | 10.1093/jb/mvae029 |