1dep

Revision as of 14:06, 20 November 2007 by OCA (talk | contribs) (New page: left|200px<br /><applet load="1dep" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dep" /> '''MEMBRANE PROTEIN, NMR, 1 STRUCTURE'''<br /> ...)
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MEMBRANE PROTEIN, NMR, 1 STRUCTURE

File:1dep.gif


1dep

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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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