1dep: Difference between revisions

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-[[Image:1dep.png|left|200px]]
-{{STRUCTURE_1dep|  PDB=1dep  |  SCENE=  }}
+==MEMBRANE PROTEIN, NMR, 1 STRUCTURE==
+<StructureSection load='1dep' size='340' side='right'caption='[[1dep]]' scene=''>
+== Structural highlights ==
+<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>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
+<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>
+</table>
+== 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.
+<div style="background-color:#fffaf0;">
+== 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>
-{{ABSTRACT_PUBMED_7828722}}
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-==About this Structure==
+<div class="pdbe-citations 1dep" style="background-color:#fffaf0;"></div>
-[[1dep]] is a 1 chain structure with 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].
 ==See Also==
-*[[Adrenergic receptor|Adrenergic receptor]]
+*[[Adrenergic receptor 3D structures|Adrenergic receptor 3D structures]]
+== References ==
-==Reference==
+<references/>
-<ref group="xtra">PMID:007828722</ref><references group="xtra"/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
 [[Category: Meleagris gallopavo]]
-[[Category: Jung, H.]]
+[[Category: Jung H]]
-[[Category: Schnackerz, K D.]]
+[[Category: Schnackerz KD]]
-[[Category: Beta-adrenoceptor]]
-[[Category: Membrane protein]]
-[[Category: Micelle-bound peptide]]