View source for 7vvn


==PTH-bound human PTH1R in complex with Gs (class4)==
<StructureSection load='7vvn' size='340' side='right'caption='[[7vvn]], [[Resolution|resolution]] 3.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7vvn]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus], [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens], [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] and [https://en.wikipedia.org/wiki/Unidentified Unidentified]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7VVN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7VVN 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]] 3.8&#8491;</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=7vvn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7vvn OCA], [https://pdbe.org/7vvn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7vvn RCSB], [https://www.ebi.ac.uk/pdbsum/7vvn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7vvn ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Endogenous parathyroid hormone (PTH) and PTH-related peptide (PTHrP) bind to the parathyroid hormone receptor 1 (PTH1R) and activate the stimulatory G-protein (Gs) signaling pathway. Intriguingly, the two ligands have distinct signaling and physiological properties: PTH evokes prolonged Gs activation, whereas PTHrP evokes transient Gs activation with reduced bone-resorption effects. The distinct molecular actions are ascribed to the differences in ligand recognition and dissociation kinetics. Here, we report cryoelectron microscopic structures of six forms of the human PTH1R-Gs complex in the presence of PTH or PTHrP at resolutions of 2.8 -4.1 A. A comparison of the PTH-bound and PTHrP-bound structures reveals distinct ligand-receptor interactions underlying the ligand affinity and selectivity. Furthermore, five distinct PTH-bound structures, combined with computational analyses, provide insights into the unique and complex process of ligand dissociation from the receptor and shed light on the distinct durations of signaling induced by PTH and PTHrP.

Endogenous ligand recognition and structural transition of a human PTH receptor.,Kobayashi K, Kawakami K, Kusakizako T, Miyauchi H, Tomita A, Kobayashi K, Shihoya W, Yamashita K, Nishizawa T, Kato HE, Inoue A, Nureki O Mol Cell. 2022 Sep 15;82(18):3468-3483.e5. doi: 10.1016/j.molcel.2022.07.003. , Epub 2022 Aug 5. PMID:35932760<ref>PMID:35932760</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7vvn" style="background-color:#fffaf0;"></div>

==See Also==
*[[Transducin 3D structures|Transducin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bos taurus]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Rattus norvegicus]]
[[Category: Unidentified]]
[[Category: Kato HE]]
[[Category: Kobayashi K]]
[[Category: Kusakizako T]]
[[Category: Miyauchi H]]
[[Category: Nishizawa T]]
[[Category: Nureki O]]
[[Category: Shihoya W]]
[[Category: Tomita A]]
[[Category: Yamashita K]]