1dep: Difference between revisions

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


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==MEMBRANE PROTEIN, NMR, 1 STRUCTURE==
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<StructureSection load='1dep' size='340' side='right'caption='[[1dep]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1dep]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Meleagris_gallopavo Meleagris gallopavo]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DEP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DEP FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1dep FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dep OCA], [https://pdbe.org/1dep PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dep RCSB], [https://www.ebi.ac.uk/pdbsum/1dep PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dep ProSAT]</span></td></tr>
{{STRUCTURE_1dep|  PDB=1dep  |  SCENE=  }}
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== Function ==
[https://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 ==
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.


===MEMBRANE PROTEIN, NMR, 1 STRUCTURE===
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<ref>PMID:7828722</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 1dep" style="background-color:#fffaf0;"></div>


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==See Also==
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*[[Adrenergic receptor 3D structures|Adrenergic receptor 3D structures]]
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== References ==
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</StructureSection>
==About this Structure==
[[Category: Large Structures]]
1DEP is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Meleagris_gallopavo Meleagris gallopavo]. Full experimental 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: Meleagris gallopavo]]
[[Category: Single protein]]
[[Category: Jung H]]
[[Category: Jung, H.]]
[[Category: Schnackerz KD]]
[[Category: Schnackerz, K D.]]
[[Category: Beta-adrenoceptor]]
[[Category: Membrane protein]]
[[Category: Micelle-bound peptide]]
 
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