View source for 1dep

[[Image:1dep.gif|left|200px]]

 {{Structure
|PDB= 1dep |SIZE=350|CAPTION= <scene name='initialview01'>1dep</scene>
|SITE= 
|LIGAND= 
|ACTIVITY= 
|GENE= 
}}

'''MEMBRANE PROTEIN, NMR, 1 STRUCTURE'''


==Overview==
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 Structure==
1DEP is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Meleagris_gallopavo Meleagris gallopavo]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DEP OCA]. 

==Reference==
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:[http://www.ncbi.nlm.nih.gov/pubmed/7828722 7828722]
[[Category: Meleagris gallopavo]]
[[Category: Single protein]]
[[Category: Jung, H.]]
[[Category: Schnackerz, K D.]]
[[Category: beta-adrenoceptor]]
[[Category: membrane protein]]
[[Category: micelle-bound peptide]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:37:21 2008''