{"id":248,"date":"2017-10-31T13:48:25","date_gmt":"2017-10-31T17:48:25","guid":{"rendered":"https:\/\/health.uconn.edu\/structural-biology\/?page_id=248"},"modified":"2017-11-03T15:31:55","modified_gmt":"2017-11-03T19:31:55","slug":"agrin-g3","status":"publish","type":"page","link":"https:\/\/health.uconn.edu\/structural-biology\/protein-structures\/agrin-g3\/","title":{"rendered":"Agrin-G3"},"content":{"rendered":"<div id=\"pl-248\"  class=\"panel-layout\" ><div id=\"pg-248-0\"  class=\"panel-grid panel-no-style\" ><div id=\"pgc-248-0-0\"  class=\"panel-grid-cell\" ><div id=\"panel-248-0-0-0\" class=\"so-panel widget widget_black-studio-tinymce widget_black_studio_tinymce panel-first-child panel-last-child\" data-index=\"0\" ><div class=\"textwidget\"><p><div style=\"width: 400px;\" class=\"wp-video\"><!--[if lt IE 9]><script>document.createElement('video');<\/script><![endif]-->\n<video class=\"wp-video-shortcode\" id=\"video-248-1\" width=\"400\" height=\"360\" loop=\"1\" autoplay=\"1\" preload=\"metadata\" controls=\"controls\"><source type=\"video\/mp4\" src=\"https:\/\/health.uconn.edu\/structural-biology\/wp-content\/uploads\/sites\/177\/2017\/11\/Agrin-G3-1.mp4?_=1\" \/><a href=\"https:\/\/health.uconn.edu\/structural-biology\/wp-content\/uploads\/sites\/177\/2017\/11\/Agrin-G3-1.mp4\">https:\/\/health.uconn.edu\/structural-biology\/wp-content\/uploads\/sites\/177\/2017\/11\/Agrin-G3-1.mp4<\/a><\/video><\/div><\/p>\n<\/div><\/div><\/div><div id=\"pgc-248-0-1\"  class=\"panel-grid-cell\" ><div class=\"panel-cell-style panel-cell-style-for-248-0-1\" ><div id=\"panel-248-0-1-0\" class=\"so-panel widget widget_black-studio-tinymce widget_black_studio_tinymce panel-first-child panel-last-child\" data-index=\"1\" ><div class=\"textwidget\"><p>Agrin is a ~600 kDa extracellular matrix proteoglycan that induces \"aggregation\" of acetylcholine receptors (AChRs) on the postsynaptic membranes of neuromuscular junctions. The C-terminus of agrin has three laminin-like globular domains, G1-G3. Agrin-G3 is the domain responsible for AChR clustering. Alternative mRNA splicing of the agrin gene results in several isoforms. The 'B' isoforms differ by inserts in the agrin-G3 domain. Isoforms with inserts are specifically expressed in neurons and induce AChR clustering. The solution structure of the B0 isoform of agrin-G3 is shown. NMR studies indicate that both the B0 and the neural B8 isoforms bind calcium. The unique perspective on agrin-G3 provided by NMR is of a domain with a versatile, flexible interaction interface that has its dynamics modulated by calcium and sequence inserts.<\/p>\n<hr \/>\n<p>Stetefeld J, Alexandrescu AT, Maciejewski MW, Jenny M, Rathgeb-Szabo K, Schulthess T, Landwehr R, Frank S, Ruegg MA, Kammerer RA (2004) Modulation of agrin function by alternative splicing and Ca2+ binding.\u00a0<em>Structure<\/em>\u00a012, 503-15.<\/p>\n<p><a href=\"http:\/\/www.ncbi.nlm.nih.gov\/entrez\/query.fcgi?cmd=Retrieve&amp;db=pubmed&amp;dopt=Abstract&amp;list_uids=15016366\">PubMed<\/a>\u00a0|\u00a0<a href=\"http:\/\/www.rcsb.org\/pdb\/cgi\/explore.cgi?pid=179571101313644&amp;page=0&amp;pdbId=1Q56\" class=\"broken_link\">PDB Link<\/a><\/p>\n<p>Alexandrescu AT, Maciejewski MW, Ruegg MA, Engel J, Kammerer RA (2001) 1H, 13C and 15N backbone assignments for the C-terminal globular domain of agrin.\u00a0<em>J Biomol NMR\u00a0<\/em>20, 295-6.<\/p>\n<p><a href=\"http:\/\/www.ncbi.nlm.nih.gov\/entrez\/query.fcgi?cmd=Retrieve&amp;db=pubmed&amp;dopt=Abstract&amp;list_uids=11519755\">PubMed<\/a><\/p>\n<p><a href=\"https:\/\/health.uconn.edu\/structural-biology\/protein-structures\/\">Back to Image Gallery<\/a><\/p>\n<\/div><\/div><\/div><\/div><\/div><\/div>","protected":false},"excerpt":{"rendered":"<p>Agrin is a ~600 kDa extracellular matrix proteoglycan that induces &#8220;aggregation&#8221; of acetylcholine receptors (AChRs) on the postsynaptic membranes of neuromuscular junctions. The C-terminus of agrin has three laminin-like globular domains, G1-G3. Agrin-G3 is the domain responsible for AChR clustering. Alternative mRNA splicing of the agrin gene results in several isoforms. The &#8216;B&#8217; isoforms differ [&hellip;]<\/p>\n","protected":false},"author":38,"featured_media":0,"parent":155,"menu_order":0,"comment_status":"closed","ping_status":"closed","template":"","meta":{"_acf_changed":false,"footnotes":""},"acf":[],"publishpress_future_action":{"enabled":false,"date":"2026-04-29 18:41:19","action":"change-status","newStatus":"draft","terms":[],"taxonomy":""},"_links":{"self":[{"href":"https:\/\/health.uconn.edu\/structural-biology\/wp-json\/wp\/v2\/pages\/248"}],"collection":[{"href":"https:\/\/health.uconn.edu\/structural-biology\/wp-json\/wp\/v2\/pages"}],"about":[{"href":"https:\/\/health.uconn.edu\/structural-biology\/wp-json\/wp\/v2\/types\/page"}],"author":[{"embeddable":true,"href":"https:\/\/health.uconn.edu\/structural-biology\/wp-json\/wp\/v2\/users\/38"}],"replies":[{"embeddable":true,"href":"https:\/\/health.uconn.edu\/structural-biology\/wp-json\/wp\/v2\/comments?post=248"}],"version-history":[{"count":15,"href":"https:\/\/health.uconn.edu\/structural-biology\/wp-json\/wp\/v2\/pages\/248\/revisions"}],"predecessor-version":[{"id":534,"href":"https:\/\/health.uconn.edu\/structural-biology\/wp-json\/wp\/v2\/pages\/248\/revisions\/534"}],"up":[{"embeddable":true,"href":"https:\/\/health.uconn.edu\/structural-biology\/wp-json\/wp\/v2\/pages\/155"}],"wp:attachment":[{"href":"https:\/\/health.uconn.edu\/structural-biology\/wp-json\/wp\/v2\/media?parent=248"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}