7w2g: Difference between revisions
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==An open-like conformation of the sigma-1 receptor from Xenopus laevis complexed with PRE084 by soaking== | ==An open-like conformation of the sigma-1 receptor from Xenopus laevis complexed with PRE084 by soaking== | ||
<StructureSection load='7w2g' size='340' side='right'caption='[[7w2g]]' scene=''> | <StructureSection load='7w2g' size='340' side='right'caption='[[7w2g]], [[Resolution|resolution]] 2.85Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7W2G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7W2G FirstGlance]. <br> | <table><tr><td colspan='2'>[[7w2g]] is a 12 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7W2G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7W2G FirstGlance]. <br> | ||
</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=7w2g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7w2g OCA], [https://pdbe.org/7w2g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7w2g RCSB], [https://www.ebi.ac.uk/pdbsum/7w2g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7w2g ProSAT]</span></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BOG:B-OCTYLGLUCOSIDE'>BOG</scene>, <scene name='pdbligand=E84:2-morpholin-4-ylethyl+1-phenylcyclohexane-1-carboxylate'>E84</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=7w2g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7w2g OCA], [https://pdbe.org/7w2g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7w2g RCSB], [https://www.ebi.ac.uk/pdbsum/7w2g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7w2g ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[[https://www.uniprot.org/uniprot/SGMR1_XENLA SGMR1_XENLA]] May function in lipid transport from the endoplasmic reticulum and be involved in a wide array of cellular functions probably through regulation of the biogenesis of lipid microdomains at the plasma membrane. May regulate calcium efflux at the endoplasmic reticulum (By similarity). | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The sigma-1 receptor (sigma1R) is a non-opioid transmembrane receptor which has been implicated in many diseases, including neurodegenerative disorders and cancer. After more than forty years of research, substantial progress has been made in understanding this unique receptor, yet the molecular mechanism of its ligand entry pathway remains uncertain. Published structures of human sigma1R reveal its homotrimeric organization of a cupin-fold beta-barrel body that contains the ligand binding site, a carboxy-terminal V-shaped two-helix bundle, and a single amino-terminal transmembrane helix, while simulation studies have suggested a ligand entry pathway that is generated by conformational rearrangements of the cupin-fold domain. Here, we present multiple crystal structures, including an open-like conformation, of sigma1R from Xenopus laevis. Together with functional binding analysis our data suggest that access to the sigma1R ligand binding site is likely achieved by protein conformational changes that involve the carboxy-terminal two-helix bundle, rather than structural changes in the cupin-fold domain. | |||
An open-like conformation of the sigma-1 receptor reveals its ligand entry pathway.,Meng F, Xiao Y, Ji Y, Sun Z, Zhou X Nat Commun. 2022 Mar 10;13(1):1267. doi: 10.1038/s41467-022-28946-w. PMID:35273182<ref>PMID:35273182</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7w2g" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Meng F]] | [[Category: Meng, F]] | ||
[[Category: Sun Z]] | [[Category: Sun, Z]] | ||
[[Category: Zhou X]] | [[Category: Zhou, X]] | ||
[[Category: Ligand entry]] | |||
[[Category: Membrane protein]] | |||
[[Category: Membrane receptor]] | |||
[[Category: S1r]] | |||
[[Category: Sigma receptor]] | |||
Revision as of 15:03, 23 March 2022
An open-like conformation of the sigma-1 receptor from Xenopus laevis complexed with PRE084 by soakingAn open-like conformation of the sigma-1 receptor from Xenopus laevis complexed with PRE084 by soaking
Structural highlights
Function[SGMR1_XENLA] May function in lipid transport from the endoplasmic reticulum and be involved in a wide array of cellular functions probably through regulation of the biogenesis of lipid microdomains at the plasma membrane. May regulate calcium efflux at the endoplasmic reticulum (By similarity). Publication Abstract from PubMedThe sigma-1 receptor (sigma1R) is a non-opioid transmembrane receptor which has been implicated in many diseases, including neurodegenerative disorders and cancer. After more than forty years of research, substantial progress has been made in understanding this unique receptor, yet the molecular mechanism of its ligand entry pathway remains uncertain. Published structures of human sigma1R reveal its homotrimeric organization of a cupin-fold beta-barrel body that contains the ligand binding site, a carboxy-terminal V-shaped two-helix bundle, and a single amino-terminal transmembrane helix, while simulation studies have suggested a ligand entry pathway that is generated by conformational rearrangements of the cupin-fold domain. Here, we present multiple crystal structures, including an open-like conformation, of sigma1R from Xenopus laevis. Together with functional binding analysis our data suggest that access to the sigma1R ligand binding site is likely achieved by protein conformational changes that involve the carboxy-terminal two-helix bundle, rather than structural changes in the cupin-fold domain. An open-like conformation of the sigma-1 receptor reveals its ligand entry pathway.,Meng F, Xiao Y, Ji Y, Sun Z, Zhou X Nat Commun. 2022 Mar 10;13(1):1267. doi: 10.1038/s41467-022-28946-w. PMID:35273182[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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