2022
DOI: 10.1016/j.cell.2022.09.041
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Molecular recognition of morphine and fentanyl by the human μ-opioid receptor

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Cited by 93 publications
(104 citation statements)
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“…In the ET B -G i complex, the downward movements of the residues are larger than those in the ET-1-bound crystal structure (Figure 2B), resulting in the outward displacement of the intracellular portion of transmembrane helix (TM) 6 by 6.8 Å as compared to the apo state (Figure 2C), and by 5.1 Å as compared to the ET-1-bound crystal structure (Figure 2D). The observed TM6 opening is smaller than those in other G i -coupled receptors (e.g., μOR: 10 Å, CB 1 : 11.6 Å, and S1P 1 : 9 Å) 30,32,33 .…”
Section: Resultsmentioning
confidence: 57%
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“…In the ET B -G i complex, the downward movements of the residues are larger than those in the ET-1-bound crystal structure (Figure 2B), resulting in the outward displacement of the intracellular portion of transmembrane helix (TM) 6 by 6.8 Å as compared to the apo state (Figure 2C), and by 5.1 Å as compared to the ET-1-bound crystal structure (Figure 2D). The observed TM6 opening is smaller than those in other G i -coupled receptors (e.g., μOR: 10 Å, CB 1 : 11.6 Å, and S1P 1 : 9 Å) 30,32,33 .…”
Section: Resultsmentioning
confidence: 57%
“…The D 3.49 R 3.50 Y 3.51 motif is conserved in the ET B receptor. Upon receptor activation, the ionic lock between D198 3.49 and R199 3.50 is broken, and R199 3.50 becomes oriented toward the intracellular cavity (Figure 2E), as in other GPCRs 32,3438 (Figure 2F, G). In contrast, the N 7.49 P 7.50 xxY 7.53 motif is altered to N 7.49 P 7.50 xxL 7.53 Y 7.54 , in which Y 7.53 is replaced by L386 7.53 .…”
Section: Resultsmentioning
confidence: 83%
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