All Outputs (3)

Pharmacological analysis and structure determination of 7-methylcyanopindolol–bound b1-adrenergic receptor (2015)
Journal Article

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.

Negative cooperativity across ?1-adrenoceptor homodimers provides insights into the nature of the secondary low-affinity CGP 12177 ?1-adrenoceptor binding conformation (2015)
Journal Article

At the β1-adrenoceptor, CGP 12177 potently antagonizes agonist responses at the primary high-affinity catecholamine conformation while also exerting agonist effects of its own through a secondary low-affinity conformation. A recent mutagenesis study... Read More about Negative cooperativity across ?1-adrenoceptor homodimers provides insights into the nature of the secondary low-affinity CGP 12177 ?1-adrenoceptor binding conformation.

Salmeterol's extreme b2 selectivity is due to residues in both extracellular loops and transmembrane domains (2015)
Journal Article

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.