7sc0: Difference between revisions
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==CryoEM structure of the Caveolin-1 8S complex== | ==CryoEM structure of the Caveolin-1 8S complex== | ||
<StructureSection load='7sc0' size='340' side='right'caption='[[7sc0]]' scene=''> | <StructureSection load='7sc0' size='340' side='right'caption='[[7sc0]], [[Resolution|resolution]] 3.40Å' 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=7SC0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7SC0 FirstGlance]. <br> | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7SC0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7SC0 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=7sc0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7sc0 OCA], [https://pdbe.org/7sc0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7sc0 RCSB], [https://www.ebi.ac.uk/pdbsum/7sc0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7sc0 ProSAT]</span></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.4Å</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=7sc0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7sc0 OCA], [https://pdbe.org/7sc0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7sc0 RCSB], [https://www.ebi.ac.uk/pdbsum/7sc0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7sc0 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Membrane-sculpting proteins shape the morphology of cell membranes and facilitate remodeling in response to physiological and environmental cues. Complexes of the monotopic membrane protein caveolin function as essential curvature-generating components of caveolae, flask-shaped invaginations that sense and respond to plasma membrane tension. However, the structural basis for caveolin's membrane remodeling activity is currently unknown. Here, we show that, using cryo-electron microscopy, the human caveolin-1 complex is composed of 11 protomers organized into a tightly packed disc with a flat membrane-embedded surface. The structural insights suggest a previously unrecognized mechanism for how membrane-sculpting proteins interact with membranes and reveal how key regions of caveolin-1, including its scaffolding, oligomerization, and intramembrane domains, contribute to its function. | |||
Molecular architecture of the human caveolin-1 complex.,Porta JC, Han B, Gulsevin A, Chung JM, Peskova Y, Connolly S, Mchaourab HS, Meiler J, Karakas E, Kenworthy AK, Ohi MD Sci Adv. 2022 May 13;8(19):eabn7232. doi: 10.1126/sciadv.abn7232. Epub 2022 May, 11. PMID:35544577<ref>PMID:35544577</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7sc0" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Latest revision as of 05:50, 5 June 2024
CryoEM structure of the Caveolin-1 8S complex
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