8flu: Difference between revisions

New page: '''Unreleased structure''' The entry 8flu is ON HOLD Authors: Description: Category: Unreleased Structures
 
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'''Unreleased structure'''


The entry 8flu is ON HOLD
==Human PTH1R in complex with LA-PTH and Gs==
<StructureSection load='8flu' size='340' side='right'caption='[[8flu]], [[Resolution|resolution]] 2.76&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8flu]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens], [https://en.wikipedia.org/wiki/Lama_glama Lama glama] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8FLU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8FLU 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]] 2.76&#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=8flu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8flu OCA], [https://pdbe.org/8flu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8flu RCSB], [https://www.ebi.ac.uk/pdbsum/8flu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8flu ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The parathyroid hormone (PTH) 1 receptor (PTH1R) is a G protein-coupled receptor (GPCR) that regulates skeletal development and calcium homeostasis. Here, we describe cryo-EM structures of the PTH1R in complex with fragments of the two hormones, PTH and PTH-related protein, the drug abaloparatide, as well as the engineered tool compounds, long-acting PTH (LA-PTH) and the truncated peptide, M-PTH(1-14). We found that the critical N terminus of each agonist engages the transmembrane bundle in a topologically similar fashion, reflecting similarities in measures of Galphas activation. The full-length peptides induce subtly different extracellular domain (ECD) orientations relative to the transmembrane domain. In the structure bound to M-PTH, the ECD is unresolved, demonstrating that the ECD is highly dynamic when unconstrained by a peptide. High resolutions enabled identification of water molecules near peptide and G protein binding sites. Our results illuminate the action of orthosteric agonists of the PTH1R.


Authors:  
Molecular insights into peptide agonist engagement with the PTH receptor.,Cary BP, Gerrard EJ, Belousoff MJ, Fletcher MM, Jiang Y, Russell IC, Piper SJ, Wootten D, Sexton PM Structure. 2023 Jun 1;31(6):668-676.e5. doi: 10.1016/j.str.2023.04.002. Epub 2023 , May 5. PMID:37148874<ref>PMID:37148874</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 8flu" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Transducin 3D structures|Transducin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Lama glama]]
[[Category: Large Structures]]
[[Category: Synthetic construct]]
[[Category: Belousoff MJ]]
[[Category: Cary BP]]
[[Category: Piper SJ]]
[[Category: Sexton PM]]
[[Category: Wootten D]]

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