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8w1z
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of a LGR dimer from Caenorhabditis elegans in apo state== | |
| + | <StructureSection load='8w1z' size='340' side='right'caption='[[8w1z]], [[Resolution|resolution]] 3.79Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[8w1z]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8W1Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8W1Z 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]] 3.79Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CLR:CHOLESTEROL'>CLR</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=8w1z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8w1z OCA], [https://pdbe.org/8w1z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8w1z RCSB], [https://www.ebi.ac.uk/pdbsum/8w1z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8w1z ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/G5EG04_CAEEL G5EG04_CAEEL] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Glycoprotein hormones (GpHs) produced in the human pituitary act through receptors (GpHRs) in the gonads to support reproduction and in the thyroid for metabolism. GpHs are heterodimeric cystine-knot proteins; their receptors bind cognate hormones at an extracellular domain and signal through a transmembrane domain to heterotrimeric G proteins. GpHs and GpHRs have co-evolved from invertebrate counterparts. Structures of the human receptors as isolated for cryogenic electron microscopy (cryo-EM) are all monomeric despite compelling evidence for their functioning as dimers. Here we characterize the homologous receptor from Caenorhabditis elegans. Its biochemical properties are notably similar to those of the thyroid stimulating hormone receptor (TSHR) of humans. Structurally, it is an asymmetric dimer (protomers screw-transformed by 142 degrees /4.1 A), composed such that only one hormone could bind. This is compatible with the 1:2 asymmetry of negatively cooperative TSH:TSHR complexes and for the transactivation evident from functional complementation of binding-deficient and signaling-deficient GpHRs. By modeling, a symmetrized dimer can bind two hormones as in the 2:2 complexes that support TSHR switches in G-protein usage. | ||
| - | + | Structure of an LGR dimer, an evolutionary predecessor of glycoprotein hormone receptors.,Gong Z, Chen S, Fu Z, Kloss B, Wang C, Kim J, Clarke OB, Fan QR, Hendrickson WA Nat Commun. 2025 Nov 28. doi: 10.1038/s41467-025-66676-x. PMID:41315418<ref>PMID:41315418</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 8w1z" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Caenorhabditis elegans]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Gong Z]] | ||
| + | [[Category: Hendrickson WA]] | ||
Current revision
Structure of a LGR dimer from Caenorhabditis elegans in apo state
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