{"id":26851,"date":"2023-07-10T15:37:56","date_gmt":"2023-07-10T19:37:56","guid":{"rendered":"https:\/\/www.med.unc.edu\/biochem\/?p=26851"},"modified":"2023-07-10T15:51:38","modified_gmt":"2023-07-10T19:51:38","slug":"baker-lab-uses-nanodiscs-to-solve-structures-of-peripheral-membrane-proteins","status":"publish","type":"post","link":"https:\/\/www.med.unc.edu\/biochem\/news\/baker-lab-uses-nanodiscs-to-solve-structures-of-peripheral-membrane-proteins\/","title":{"rendered":"Baker lab uses nanodiscs to solve structures of peripheral membrane proteins!"},"content":{"rendered":"<p><span class=\"TextRun SCXW188285348 BCX0\" lang=\"EN-US\" xml:lang=\"EN-US\" data-contrast=\"auto\"><span class=\"NormalTextRun SCXW188285348 BCX0\">Congratulations to the <\/span><\/span><span class=\"TextRun SCXW188285348 BCX0\" lang=\"EN-US\" xml:lang=\"EN-US\" data-contrast=\"auto\"><span class=\"NormalTextRun SCXW188285348 BCX0\">Baker lab<\/span><\/span><span class=\"TextRun SCXW188285348 BCX0\" lang=\"EN-US\" xml:lang=\"EN-US\" data-contrast=\"auto\"><span class=\"NormalTextRun SCXW188285348 BCX0\"> on their amazing work using <\/span><span class=\"NormalTextRun SCXW188285348 BCX0\">nanodiscs<\/span><span class=\"NormalTextRun SCXW188285348 BCX0\"> to solve structures of peripheral membrane proteins is now available online in the<\/span><\/span> <a class=\"Hyperlink SCXW188285348 BCX0\" href=\"https:\/\/www.sciencedirect.com\/science\/article\/pii\/S1047847723000527?dgcid=author\" target=\"_blank\" rel=\"noreferrer noopener\"><span class=\"TextRun Underlined SCXW188285348 BCX0\" lang=\"EN-US\" xml:lang=\"EN-US\" data-contrast=\"none\"><span class=\"NormalTextRun SCXW188285348 BCX0\" data-ccp-charstyle=\"Hyperlink\">Journal of Structural Biology<\/span><\/span><\/a><span class=\"TextRun SCXW188285348 BCX0\" lang=\"EN-US\" xml:lang=\"EN-US\" data-contrast=\"auto\"><span class=\"NormalTextRun SCXW188285348 BCX0\">.\u00a0<\/span><\/span><span class=\"TextRun SCXW188285348 BCX0\" lang=\"EN-US\" xml:lang=\"EN-US\" data-contrast=\"auto\"><span class=\"NormalTextRun SCXW188285348 BCX0\"> Thank you to Postdocs <\/span><\/span><span class=\"TextRun SCXW188285348 BCX0\" lang=\"EN-US\" xml:lang=\"EN-US\" data-contrast=\"auto\"><span class=\"NormalTextRun SCXW188285348 BCX0\">Kevin Cannon<\/span><\/span><span class=\"TextRun SCXW188285348 BCX0\" lang=\"EN-US\" xml:lang=\"EN-US\" data-contrast=\"auto\"><span class=\"NormalTextRun SCXW188285348 BCX0\"> and <\/span><\/span><span class=\"TextRun SCXW188285348 BCX0\" lang=\"EN-US\" xml:lang=\"EN-US\" data-contrast=\"auto\"><span class=\"NormalTextRun SCXW188285348 BCX0\">Reta <\/span><span class=\"NormalTextRun SCXW188285348 BCX0\">Sarsam<\/span><\/span><span class=\"TextRun SCXW188285348 BCX0\" lang=\"EN-US\" xml:lang=\"EN-US\" data-contrast=\"auto\"><span class=\"NormalTextRun SCXW188285348 BCX0\"> for their hard work! This research will be published in the September issue of JSB<\/span><span class=\"NormalTextRun SCXW188285348 BCX0\">.<\/span><\/span><\/p>\n<p><img loading=\"lazy\" decoding=\"async\" class=\"size-medium wp-image-26858 aligncenter\" src=\"https:\/\/www.med.unc.edu\/biochem\/wp-content\/uploads\/sites\/795\/2023\/07\/rick-baker-at-conference-7-2023-300x225.jpg\" alt=\"dr rick baker at conference 7-2023\" width=\"300\" height=\"225\" srcset=\"https:\/\/www.med.unc.edu\/biochem\/wp-content\/uploads\/sites\/795\/2023\/07\/rick-baker-at-conference-7-2023-300x225.jpg 300w, https:\/\/www.med.unc.edu\/biochem\/wp-content\/uploads\/sites\/795\/2023\/07\/rick-baker-at-conference-7-2023-1024x768.jpg 1024w, https:\/\/www.med.unc.edu\/biochem\/wp-content\/uploads\/sites\/795\/2023\/07\/rick-baker-at-conference-7-2023-768x576.jpg 768w, https:\/\/www.med.unc.edu\/biochem\/wp-content\/uploads\/sites\/795\/2023\/07\/rick-baker-at-conference-7-2023-1536x1152.jpg 1536w, https:\/\/www.med.unc.edu\/biochem\/wp-content\/uploads\/sites\/795\/2023\/07\/rick-baker-at-conference-7-2023-2048x1536.jpg 2048w, https:\/\/www.med.unc.edu\/biochem\/wp-content\/uploads\/sites\/795\/2023\/07\/rick-baker-at-conference-7-2023-280x210.jpg 280w, https:\/\/www.med.unc.edu\/biochem\/wp-content\/uploads\/sites\/795\/2023\/07\/rick-baker-at-conference-7-2023-600x450.jpg 600w, https:\/\/www.med.unc.edu\/biochem\/wp-content\/uploads\/sites\/795\/2023\/07\/rick-baker-at-conference-7-2023-560x420.jpg 560w\" sizes=\"auto, (max-width: 300px) 100vw, 300px\" \/><\/p>\n<p>Lay Summary<\/p>\n<p>There are over one hundred thousand structures deposited into the protein data bank. Despite this, there are only a handful of structures of proteins bound to membranes. In this paper, members of the Baker lab use cryoEM and membrane platforms called nanodiscs as a way to solve high-resolution structures of proteins that transiently engage the membrane.<\/p>\n<p>Abstract<\/p>\n<p>Peripheral membrane proteins\u00a0are ubiquitous throughout cell biology and are required for a variety of cellular processes such as\u00a0signal transduction, membrane trafficking, and autophagy. Transient binding to the membrane has a profound impact on protein function, serving to induce conformational changes and alter biochemical and biophysical parameters by increasing the local concentration of factors and restricting diffusion to two dimensions. Despite the centrality of the membrane in serving as a template for cell biology, there are few reported high-resolution structures of peripheral membrane proteins bound to the membrane. We analyzed the utility of\u00a0lipid\u00a0nanodiscs to serve as a template for cryo-EM analysis of peripheral membrane proteins. We tested a variety of nanodiscs and we report a 3.3\u00a0\u00c5 structure of the AP2\u00a0clathrin\u00a0adaptor complex bound to a 17-nm nanodisc, with sufficient resolution to visualize a bound lipid head group. Our data demonstrate that lipid nanodiscs are amenable to high-resolution structure determination of peripheral membrane proteins and provide a framework for extending this analysis to other systems.<\/p>\n<p>Publication link<\/p>\n<p>Kevin S. Cannon, Reta D. Sarsam, Tanita Tedamrongwanish, Kevin Zhang, Richard W. Baker,<br \/>\n<a href=\"https:\/\/www.sciencedirect.com\/science\/article\/pii\/S1047847723000527\">Lipid nanodiscs as a template for high-resolution cryo-EM structures of peripheral membrane proteins<\/a>,<br \/>\nJournal of Structural Biology,<br \/>\nVolume 215, Issue 3, 2023,107989, ISSN 1047-8477.<\/p>\n","protected":false},"excerpt":{"rendered":"<p>Congratulations to the Baker lab on their amazing work using nanodiscs to solve structures of peripheral membrane proteins<\/p>\n","protected":false},"author":41619,"featured_media":26858,"comment_status":"closed","ping_status":"closed","sticky":false,"template":"","format":"standard","meta":{"_acf_changed":false,"layout":"","cellInformation":"","apiCallInformation":"","footnotes":"","_links_to":"","_links_to_target":""},"categories":[2],"tags":[10,385,179],"class_list":["post-26851","post","type-post","status-publish","format-standard","has-post-thumbnail","hentry","category-news","tag-news_faculty","tag-news_2023","tag-news_postdoc-scholars","odd"],"acf":[],"yoast_head":"<!-- This site is optimized with the Yoast SEO plugin v26.8 - https:\/\/yoast.com\/product\/yoast-seo-wordpress\/ -->\n<title>Baker lab uses nanodiscs to solve structures of peripheral membrane proteins! 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