期刊
SCIENCE
卷 372, 期 6538, 页码 147-+出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.abf7258
关键词
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资金
- Monash University Ramaciotti Centre for Cryo-Electron Microscopy
- Monash MASSIVE high-performance computing facility
- MIPS seed funding
- Australian Research Council (ARC) Centre grant [IC200100052]
- ARC Discovery Project [DP210101504]
- National Health and Medical Research Council of Australia (NHMRC) [1120919, 1159006]
- NHMRC program grant [1150083]
- Takeda Science Foundation 2019 Medical Research Grant
- Japan Science and Technology Agency PRESTO [18069571]
- Australian Research Council Future Fellowship [FT160100075]
- National Health and Medical Research Council of Australia [1159006, 1150083, 1120919] Funding Source: NHMRC
- Australian Research Council [IC200100052, FT160100075] Funding Source: Australian Research Council
This study provides insights into the mechanisms of class B1 GPCR activation by analyzing the structures and protein conformational dynamics of GPCRs.
G protein-coupled receptors (GPCRs) are key regulators of information transmission between cells and organs. Despite this, we have only a limited understanding of the behavior of GPCRs in the apo state and the conformational changes upon agonist binding that lead to G protein recruitment and activation. We expressed and purified unmodified apo and peptide-bound calcitonin gene-related peptide (CGRP) receptors from insect cells to determine their cryo-electron microscopy (cryo-EM) structures, and we complemented these with analysis of protein conformational dynamics using hydrogen-deuterium exchange mass spectrometry and three-dimensional variance analysis of the cryo-EM data. Together with our previously published structure of the active, Gs-bound CGRP receptor complex, our work provides insight into the mechanisms of class B1 GPCR activation.
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