1dep
MEMBRANE PROTEIN, NMR, 1 STRUCTURE
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OverviewOverview
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.
About this StructureAbout this Structure
1DEP is a Single protein structure of sequence from Meleagris gallopavo. Full crystallographic information is available from OCA.
ReferenceReference
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
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