Pharmacological analysis and structure determination of 7-methylcyanopindolol–bound b1-adrenergic receptor

Comparisons between structures of the b1-adrenergic receptor (AR) bound to either agonists, partial agonists, or weak partial agonists led to the proposal that rotamer changes of Ser5.46, coupled to a contraction of the binding pocket, are sufficient to increase the probability of receptor activatio...

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Main Authors: Sato, Tomomi, Baker, Jillian G., Warne, Tony, Brown, Giles A., Leslie, Andrew, Congreve, Miles, Tate, Christopher G.
Format: Article
Published: ASPET 2015
Online Access:https://eprints.nottingham.ac.uk/40727/
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author Sato, Tomomi
Baker, Jillian G.
Warne, Tony
Brown, Giles A.
Leslie, Andrew
Congreve, Miles
Tate, Christopher G.
author_facet Sato, Tomomi
Baker, Jillian G.
Warne, Tony
Brown, Giles A.
Leslie, Andrew
Congreve, Miles
Tate, Christopher G.
author_sort Sato, Tomomi
building Nottingham Research Data Repository
collection Online Access
description Comparisons between structures of the b1-adrenergic receptor (AR) bound to either agonists, partial agonists, or weak partial agonists led to the proposal that rotamer changes of Ser5.46, coupled to a contraction of the binding pocket, are sufficient to increase the probability of receptor activation. (RS)-4-[3 (tertbutylamino)-2-hydroxypropoxy]-1H-indole-2 carbonitrile (cyanopindolol) is a weak partial agonist of b1AR and, based on the hypothesis above, we predicted that the addition of a methyl group to form 4-[(2S)-3 (tert-butylamino)-2-hydroxypropoxy]-7-methyl-1H-indole-2 carbonitrile (7-methylcyanopindolol) would dramatically reduce its efficacy. An eight-step synthesis of 7- methylcyanopindolol was developed and its pharmacology was analyzed. 7-Methylcyanopindolol bound with similar affinity to cyanopindolol to both b1AR and b2AR. As predicted, the efficacy of 7-methylcyanopindolol was reduced significantly compared with cyanopindolol, acting as a very weak partial agonist of turkey b1AR and an inverse agonist of human b2AR. The structure of 7-methylcyanopindolol–bound b1AR was determined to 2.4-Å resolution and found to be virtually identical to the structure of cyanopindolol-bound b1AR. The major differences in the orthosteric binding pocket are that it has expanded by 0.3 Å in 7-methylcyanopindolol–bound b1AR and the hydroxyl group of Ser5.46 is positioned 0.8 Å further from the ligand, with respect to the position of the Ser5.46 side chain in cyanopindololbound b1AR. Thus, the molecular basis for the reduction in efficacy of 7 methylcyanopindolol compared with cyanopindolol may be regarded as the opposite of the mechanism proposed for the increase in efficacy of agonists compared with antagonists.
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spelling nottingham-407272020-05-04T17:25:27Z https://eprints.nottingham.ac.uk/40727/ Pharmacological analysis and structure determination of 7-methylcyanopindolol–bound b1-adrenergic receptor Sato, Tomomi Baker, Jillian G. Warne, Tony Brown, Giles A. Leslie, Andrew Congreve, Miles Tate, Christopher G. Comparisons between structures of the b1-adrenergic receptor (AR) bound to either agonists, partial agonists, or weak partial agonists led to the proposal that rotamer changes of Ser5.46, coupled to a contraction of the binding pocket, are sufficient to increase the probability of receptor activation. (RS)-4-[3 (tertbutylamino)-2-hydroxypropoxy]-1H-indole-2 carbonitrile (cyanopindolol) is a weak partial agonist of b1AR and, based on the hypothesis above, we predicted that the addition of a methyl group to form 4-[(2S)-3 (tert-butylamino)-2-hydroxypropoxy]-7-methyl-1H-indole-2 carbonitrile (7-methylcyanopindolol) would dramatically reduce its efficacy. An eight-step synthesis of 7- methylcyanopindolol was developed and its pharmacology was analyzed. 7-Methylcyanopindolol bound with similar affinity to cyanopindolol to both b1AR and b2AR. As predicted, the efficacy of 7-methylcyanopindolol was reduced significantly compared with cyanopindolol, acting as a very weak partial agonist of turkey b1AR and an inverse agonist of human b2AR. The structure of 7-methylcyanopindolol–bound b1AR was determined to 2.4-Å resolution and found to be virtually identical to the structure of cyanopindolol-bound b1AR. The major differences in the orthosteric binding pocket are that it has expanded by 0.3 Å in 7-methylcyanopindolol–bound b1AR and the hydroxyl group of Ser5.46 is positioned 0.8 Å further from the ligand, with respect to the position of the Ser5.46 side chain in cyanopindololbound b1AR. Thus, the molecular basis for the reduction in efficacy of 7 methylcyanopindolol compared with cyanopindolol may be regarded as the opposite of the mechanism proposed for the increase in efficacy of agonists compared with antagonists. ASPET 2015-12-31 Article PeerReviewed Sato, Tomomi, Baker, Jillian G., Warne, Tony, Brown, Giles A., Leslie, Andrew, Congreve, Miles and Tate, Christopher G. (2015) Pharmacological analysis and structure determination of 7-methylcyanopindolol–bound b1-adrenergic receptor. Molecular Pharmacology, 88 (6). pp. 1024-1034. ISSN 1521-0111 http://molpharm.aspetjournals.org/content/88/6/1024 doi:10.1124/mol.115.101030 doi:10.1124/mol.115.101030
spellingShingle Sato, Tomomi
Baker, Jillian G.
Warne, Tony
Brown, Giles A.
Leslie, Andrew
Congreve, Miles
Tate, Christopher G.
Pharmacological analysis and structure determination of 7-methylcyanopindolol–bound b1-adrenergic receptor
title Pharmacological analysis and structure determination of 7-methylcyanopindolol–bound b1-adrenergic receptor
title_full Pharmacological analysis and structure determination of 7-methylcyanopindolol–bound b1-adrenergic receptor
title_fullStr Pharmacological analysis and structure determination of 7-methylcyanopindolol–bound b1-adrenergic receptor
title_full_unstemmed Pharmacological analysis and structure determination of 7-methylcyanopindolol–bound b1-adrenergic receptor
title_short Pharmacological analysis and structure determination of 7-methylcyanopindolol–bound b1-adrenergic receptor
title_sort pharmacological analysis and structure determination of 7-methylcyanopindolol–bound b1-adrenergic receptor
url https://eprints.nottingham.ac.uk/40727/
https://eprints.nottingham.ac.uk/40727/
https://eprints.nottingham.ac.uk/40727/