1dep: Difference between revisions
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</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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.rcsb.org/pdb/explore.do?structureId=1dep RCSB], [http://www.ebi.ac.uk/pdbsum/1dep PDBsum]</span></td></tr> | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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.rcsb.org/pdb/explore.do?structureId=1dep RCSB], [http://www.ebi.ac.uk/pdbsum/1dep PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/ADRB1_MELGA ADRB1_MELGA]] Beta-adrenergic receptors mediate the catecholamine-induced activation of adenylate cyclase through the action of G proteins. This receptor binds epinephrine and norepinephrine with approximately equal affinity. | |||
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== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Revision as of 10:12, 25 December 2014
MEMBRANE PROTEIN, NMR, 1 STRUCTUREMEMBRANE PROTEIN, NMR, 1 STRUCTURE
Structural highlights
Function[ADRB1_MELGA] Beta-adrenergic receptors mediate the catecholamine-induced activation of adenylate cyclase through the action of G proteins. This receptor binds epinephrine and norepinephrine with approximately equal affinity. Publication Abstract from PubMedThe 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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