1DEP

MEMBRANE PROTEIN, NMR, 1 STRUCTURE

Summary for 1DEP

• Entry DOI: 10.2210/pdb1dep/pdb
• Descriptor: T345-359 (1 entity in total)
• Functional Keywords: beta-adrenoceptor, micelle-bound peptide, membrane protein
• Biological source: Meleagris gallopavo (turkey)
• Cellular location: Cell membrane; Multi-pass membrane protein: P07700
• Total number of polymer chains: 1
• Total formula weight: 1889.29

Authors

Jung, H.,Schnackerz, K.D. (deposition date: 1995-08-23, release date: 1996-10-14, Last modification date: 2024-05-22)

Primary citation

Jung, H.,Windhaber, R.,Palm, D.,Schnackerz, K.D.
NMR and circular dichroism studies of synthetic peptides derived from the third intracellular loop of the beta-adrenoceptor.
FEBS Lett., 358:133-136, 1995

PubMed Abstract: 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.

PubMed: 7828722
DOI: 10.1016/0014-5793(94)01409-T

Experimental method

SOLUTION NMR