1dep: Difference between revisions

Revision as of 13:46, 2 May 2008

MEMBRANE PROTEIN, NMR, 1 STRUCTURE

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 Page seeded by OCA on Fri May 2 13:46:11 2008

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OCA

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 [[Image:1dep.gif|left|200px]]
- {{Structure
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 '''MEMBRANE PROTEIN, NMR, 1 STRUCTURE'''
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 [[Category: Jung, H.]]
 [[Category: Schnackerz, K D.]]
-[[Category: beta-adrenoceptor]]
+[[Category: Beta-adrenoceptor]]
-[[Category: membrane protein]]
+[[Category: Membrane protein]]
-[[Category: micelle-bound peptide]]
+[[Category: Micelle-bound peptide]]
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 13:46:11 2008''
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:40:10 2008''