1dep: Difference between revisions
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dep FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dep OCA], [http://www.ebi.ac.uk/pdbsum/1dep PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1dep RCSB]</span> | |||
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[[Category: micelle-bound peptide]] | [[Category: micelle-bound peptide]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:40:10 2008'' | ||
Revision as of 19:40, 30 March 2008
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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