6p9y: Difference between revisions

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-'''Unreleased structure'''
-The entry 6p9y is ON HOLD
+==PAC1 GPCR Receptor complex==
+<SX load='6p9y' size='340' side='right' viewer='molstar' caption='[[6p9y]], [[Resolution|resolution]] 3.01&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6p9y]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Lama_glama Lama glama]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6P9Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6P9Y FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.01&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></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=6p9y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6p9y OCA], [https://pdbe.org/6p9y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6p9y RCSB], [https://www.ebi.ac.uk/pdbsum/6p9y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6p9y ProSAT]</span></td></tr>
+</table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Class B G protein-coupled receptors (GPCRs) are important therapeutic targets for major diseases. Here, we present structures of peptide and Gs-bound pituitary adenylate cyclase-activating peptide, PAC1 receptor, and corticotropin-releasing factor (CRF), (CRF1) receptor. Together with recently solved structures, these provide coverage of the major class B GPCR subfamilies. Diverse orientations of the extracellular domain to the receptor core in different receptors are at least partially dependent on evolutionary conservation in the structure and nature of peptide interactions. Differences in peptide interactions to the receptor core also influence the interlinked TM2-TM1-TM6/ECL3/TM7 domain, and this is likely important in their diverse signaling. However, common conformational reorganization of ECL2, linked to reorganization of ICL2, modulates G protein contacts. Comparison between receptors reveals ICL2 as a key domain forming dynamic G protein interactions in a receptor- and ligand-specific manner. This work advances our understanding of class B GPCR activation and Gs coupling.
-Authors:
+Toward a Structural Understanding of Class B GPCR Peptide Binding and Activation.,Liang YL, Belousoff MJ, Zhao P, Koole C, Fletcher MM, Truong TT, Julita V, Christopoulos G, Xu HE, Zhang Y, Khoshouei M, Christopoulos A, Danev R, Sexton PM, Wootten D Mol Cell. 2020 Feb 6;77(3):656-668.e5. doi: 10.1016/j.molcel.2020.01.012. Epub, 2020 Jan 30. PMID:32004469<ref>PMID:32004469</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 6p9y" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Transducin 3D structures|Transducin 3D structures]]
+== References ==
+<references/>
+__TOC__
+</SX>
+[[Category: Homo sapiens]]
+[[Category: Lama glama]]
+[[Category: Large Structures]]
+[[Category: Belousoff MJ]]
+[[Category: Danev R]]
+[[Category: Liang YL]]
+[[Category: Sexton P]]