1DEP | pdb_00001dep

NMR and circular dichroism studies of synthetic peptides derived from the third intracellular loop of the beta-adrenoceptor.

(1995) FEBS Lett 358: 133-136

• PubMed: 7828722 Search on PubMed
• DOI: https://doi.org/10.1016/0014-5793(94)01409-t
• Primary Citation of Related Structures:  
  1DEP


• 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.

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Organizational Affiliation: 

Theodor-Boveri-Institut für Biowissenschaften, Universität Würzburg, Germany.