All Outputs (2)

Pharmacological analysis and structure determination of 7-methylcyanopindolol–bound b1-adrenergic receptor (2015)
Journal Article
Sato, T., Baker, J. G., Warne, T., Brown, G. A., Leslie, A., Congreve, M., & Tate, C. G. (2015). Pharmacological analysis and structure determination of 7-methylcyanopindolol–bound b1-adrenergic receptor. Molecular Pharmacology, 88(6), https://doi.org/10.1124/mol.115.101030

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... Read More about Pharmacological analysis and structure determination of 7-methylcyanopindolol–bound b1-adrenergic receptor.

Salmeterol's extreme b2 selectivity is due to residues in both extracellular loops and transmembrane domains (2015)
Journal Article
Baker, J. G., Proudman, R. G., & Hill, S. J. (2015). Salmeterol's extreme b2 selectivity is due to residues in both extracellular loops and transmembrane domains. Molecular Pharmacology, 87(1), https://doi.org/10.1124/mol.114.095364

Salmeterol is a long-acting b2-agonist, widely used as an inhaled treatment of asthma and chronic obstructive pulmonary disease. It has very high b2-affinity (log KD 28.95) and is very selective for the b2-adrenoceptor (1000-fold selectivity over the... Read More about Salmeterol's extreme b2 selectivity is due to residues in both extracellular loops and transmembrane domains.