β1-selective agonist (-)-1-(3,4-dimethoxyphenetylamino)-3-(3,4-dihydroxy)-2-propanol [(-)-RO363] differentially interacts with key amino acids responsible for β1-selective binding in resting and active states

Journal of Pharmacology and Experimental Therapeutics

Volumn 301, Issue 1, 2002, Pages 51-58

  Sugimoto, Yoshiyuki ^a,e   Fujisawa, Reiko ^a   Tanimura, Ryuji ^b   Lattion, Anne Laure ^d   Cotecchia, Susanna ^d   Tsujimoto, Gozoh ^c   Nagao, Taku ^a   Kurose, Hitoshi ^a  

^a UNIVERSITY OF TOKYO   (Japan)

^b TORAY INDUSTRIES INC   (Japan)

^c NATIONAL RESEARCH INSTITUTE FOR CHILD HEALTH AND DEVELOPMENT   (Japan)

^d Institute de Pharmacologie et de Toxicologie   (Switzerland)

^e KYOWA HAKKO KOGYO CO LTD   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

1 (3,4 DIHYDROXYPHENOXY) 3 (3,4 DIMETHOXYPHENETHYLAMINO) 2 PROPANOL; BETA 1 ADRENERGIC RECEPTOR; RECEPTOR SUBTYPE;

AMINO ACID SUBSTITUTION; ANIMAL CELL; ARTICLE; BINDING AFFINITY; BINDING SITE; CONTROLLED STUDY; DRUG BINDING; DRUG RECEPTOR BINDING; HYDROGEN BOND; LIGAND BINDING; MOLECULAR MODEL; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN;

ADRENERGIC BETA-AGONISTS; AMINO ACID SEQUENCE; AMINO ACIDS; CATECHOLS; GENE EXPRESSION REGULATION; HUMANS; KINETICS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTATION; PLASMIDS; PROPANOLAMINES; RADIOLIGAND ASSAY; RECEPTORS, ADRENERGIC, BETA-1; RECEPTORS, ADRENERGIC, BETA-2; RECOMBINANT FUSION PROTEINS;

EID: 0036128982     PISSN: 00223565     EISSN: None     Source Type: Journal    
DOI: 10.1124/jpet.301.1.51     Document Type: Article

References (38)

1. Light-induced exposure of the cytoplasmic end of transmembrane helix seven in rhodopsin
2. 135 sequence in rhodopsin
3. An α-carbon template for the transmembrane helices in the rhodopsin family of G-protein coupled receptors
4. Functional microdomains in G-protein-coupled receptors
5. Genetic analysis of the molecular basis for β-adrenergic receptor subtype specificity
6. Ligand binding to the β-adrenoceptorergic receptor involves its rhodopsin-like core
7. 2-adrenergic receptor
8. Conserved polar residues in the transmembrane domain of the human tachykinin NK2 receptor: Functional roles and structural implications
9. Requirement of rigid-body motion of transmembrane helices for light activation of rhodopsin
10. 2-adrenergic receptors
11. G-protein coupled receptors. II. Mechanism of agonist activation
12. Agonists induce conformational changes in transmembrane domains III and VI of the β2-adrenoceptor
13. 2-adrenergic receptor ligand binding pocket
14. 2-adrenergic receptors for subtype-selective agonists
15. 2-adrenergic receptor for high affinity binding of salmeterol
16. 2-selective agonist TA-2005
17. A proposed structure for transmembrane segment 7 of G protein-coupled receptors incorporating an Asn-Pro/Asp-Pro Motif
18. 1-adrenergic receptor
19. Protein measurement with the folin phenol reagent
20. 2-adrenergic receptors involves multiple subsites
21. 2-adrenoceptor sites
22. 3-adrenoceptors
23. Interaction between conserved residues in transmembrane helices 1, 2, and 7 of the thyrotropin-releasing hormone receptor
24. 2 adrenergic receptor: Constitutive activation, structural instability, and conformational rearrangement of transmembrane segment 6
25. 2-adrenoceptor contributes to agonist binding and receptor activation
26. 1B-adrenergic receptor: Role of highly conserved polar amino acids in receptor activation
27. 1B-adrenergic receptor: Potential role of protonation and hydrophobicity of a highly conserved aspartate
28. 2A receptor
29. Rhodopsin activation blocked by metal-ion-binding sites linking transmembrane helices C and F
30. A single amino acid substitution in the β-adrenergic receptor promotes partial agonist activity from antagonists
31. Identification of two serine residues involved in agonist activation of the β-adrenergic receptor
32. Structure and function of G protein-coupled receptors
33. Identification of residues required for ligand binding to the β-adrenergic receptor
34. Conserved aspartic acid residues 79 and 113 of the β-adrenergic receptor have different roles in receptor function
35. Determinants of protein-side chain packing
36. 2-adrenergic receptor
37. 2-adrenergic receptor is formed by juxtaposed membrane-spanning domains
38. A reciprocal mutation supports halix 2 and helix 7 proximity in the gonadotropin-releasing hormone receptor