Structural highlights
Function
ADRB1_MELGA Beta-adrenergic receptors mediate the catecholamine-induced activation of adenylate cyclase through the action of G proteins. This receptor binds epinephrine and norepinephrine with approximately equal affinity.
Publication Abstract from PubMed
The C-terminal part of the third intracellular loop of the beta-adrenoceptor is capable of stimulating adenylate cyclase in the presence of phospholipid vesicles via the stimulatory guanine nucleotide binding protein (Gs) [Palm et al. (1989) FEBS Lett. 254, 89-93]. We have investigated the structure of synthetic peptides corresponding to residues 284-295 of the turkey erythrocyte adrenoceptor in micelles, trifluoroethanol and aqueous solution, by using 2D 1H NMR and CD. In the presence of phospholipid micelles the peptides display a C-terminal alpha-helical region, whereas the N-terminal part was found to be highly flexible.
NMR and circular dichroism studies of synthetic peptides derived from the third intracellular loop of the beta-adrenoceptor.,Jung H, Windhaber R, Palm D, Schnackerz KD FEBS Lett. 1995 Jan 23;358(2):133-6. PMID:7828722[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Jung H, Windhaber R, Palm D, Schnackerz KD. NMR and circular dichroism studies of synthetic peptides derived from the third intracellular loop of the beta-adrenoceptor. FEBS Lett. 1995 Jan 23;358(2):133-6. PMID:7828722
