Ligand occupancy in crystal structure of β1-adrenergic G protein–coupled receptor

Huang, Jian; Chen, Shuai; Zhang, J Jillian; Huang, Xin‐Yun

doi:10.1038/nsmb.3131

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“…One more interesting thing is the identification of a ligand-free basal state of β 1 AR, which was reported by Huang et al in 2013 . This structure was represented as the only class A nonrhodopsin structure crystallized in the ligand-free state; however, it still remains controversial after Leslie et al repeated the structure determination using the deposited structure factors and identified substantial unmodeled electron density for a ligand in the orthosteric pocket. , …”

Section: Progress In Structural Studies Of Class a Nonrhodopsin Gpcrsmentioning

confidence: 91%

“…35 This structure was represented as the only class A nonrhodopsin structure crystallized in the ligand-free state; however, it still remains controversial after Leslie et al repeated the structure determination using the deposited structure factors and identified substantial unmodeled electron density for a ligand in the orthosteric pocket. 36,37 The sequence identity between β 1 AR and β 2 AR is approximately 67% in the TM regions. Because of the high sequence identity, the overall structures of the two receptor subtypes in their inactive states are similar.…”

Section: Solved Structures Ofmentioning

confidence: 99%

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Recent Advances in Structure-Based Drug Design Targeting Class A G Protein-Coupled Receptors Utilizing Crystal Structures and Computational Simulations

2017

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G protein-coupled receptors (GPCRs) represent the largest and most physiologically important integral membrane protein family, and these receptors respond to a wide variety of physiological and environmental stimuli. GPCRs are among the most critical therapeutic targets for numerous human diseases, and approximately one-third of the currently marketed drugs target this receptor family. The recent breakthroughs in GPCR structural biology have significantly contributed to our understanding of GPCR function, ligand binding, and pharmacological action as well as to the design of new drugs. This perspective highlights the latest advances in GPCR structures with a focus on the receptor-ligand interactions of each receptor family in class A nonrhodopsin GPCRs as well as the structural features for their activation, biased signaling, and allosteric mechanisms. The current state-of-the-art methodologies of structure-based drug design (SBDD) approaches in the GPCR research field are also discussed.

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Section: Progress In Structural Studies Of Class a Nonrhodopsin Gpcrsmentioning

confidence: 91%

Section: Solved Structures Ofmentioning

confidence: 99%

Recent Advances in Structure-Based Drug Design Targeting Class A G Protein-Coupled Receptors Utilizing Crystal Structures and Computational Simulations

2017

View full text Add to dashboard Cite

show abstract

Ligand occupancy in crystal structure of β1-adrenergic G protein–coupled receptor

Cited by 1 publication

References 2 publications

Recent Advances in Structure-Based Drug Design Targeting Class A G Protein-Coupled Receptors Utilizing Crystal Structures and Computational Simulations

Recent Advances in Structure-Based Drug Design Targeting Class A G Protein-Coupled Receptors Utilizing Crystal Structures and Computational Simulations

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