{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T17:30:23Z","timestamp":1791307823467,"version":"4.3.1"},"reference-count":43,"publisher":"National Academy of Sciences","issue":"28","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2008,7,15]]},"abstract":"<jats:p>\n                    The skeletal muscle Ca\n                    <jats:sup>2+<\/jats:sup>\n                    release channel (RyR1), a homotetramer, regulates the release of Ca\n                    <jats:sup>2+<\/jats:sup>\n                    from the sarcoplasmic reticulum to initiate muscle contraction. In this work, we have delineated the RyR1 monomer boundaries in a subnanometer-resolution electron cryomicroscopy (cryo-EM) density map. In the cytoplasmic region of each RyR1 monomer, 36 \u03b1-helices and 7 \u03b2-sheets can be resolved. A \u03b2-sheet was also identified close to the membrane-spanning region that resembles the cytoplasmic pore structures of inward rectifier K\n                    <jats:sup>+<\/jats:sup>\n                    channels. Three structural folds, generated for amino acids 12\u2013565 using comparative modeling and cryo-EM density fitting, localize close to regions implicated in communication with the voltage sensor in the transverse tubules. Eleven of the 15 disease-related residues for these domains are mapped to the surface of these models. Four disease-related residues are found in a basin at the interfaces of these regions, creating a pocket in which the immunophilin FKBP12 can fit. Taken together, these results provide a structural context for both channel gating and the consequences of certain malignant hyperthermia and central core disease-associated mutations in RyR1.\n                  <\/jats:p>","DOI":"10.1073\/pnas.0803189105","type":"journal-article","created":{"date-parts":[[2008,7,10]],"date-time":"2008-07-10T21:30:37Z","timestamp":1215725437000},"page":"9610-9615","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":97,"title":["Subnanometer-resolution electron cryomicroscopy-based domain models for the cytoplasmic region of skeletal muscle RyR channel"],"prefix":"10.1073","volume":"105","author":[{"given":"Irina I.","family":"Serysheva","sequence":"first","affiliation":[{"name":"*National Center for Macromolecular Imaging, Verna and Marrs McLean Department of Biochemistry and Molecular Biology, and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Steven J.","family":"Ludtke","sequence":"additional","affiliation":[{"name":"*National Center for Macromolecular Imaging, Verna and Marrs McLean Department of Biochemistry and Molecular Biology, and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Matthew L.","family":"Baker","sequence":"additional","affiliation":[{"name":"*National Center for Macromolecular Imaging, Verna and Marrs McLean Department of Biochemistry and Molecular Biology, and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yao","family":"Cong","sequence":"additional","affiliation":[{"name":"*National Center for Macromolecular Imaging, Verna and Marrs McLean Department of Biochemistry and Molecular Biology, and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Maya","family":"Topf","sequence":"additional","affiliation":[{"name":"Department of Crystallography, Birkbeck College, University of London, Malet Street, London WC1E 7HX, United Kingdom; and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"David","family":"Eramian","sequence":"additional","affiliation":[{"name":"Departments of Biopharmaceutical Sciences and Pharmaceutical Chemistry, California Institute for Quantitative Biosciences, University of California, Mission Bay Byers Hall, 1700 Fourth Street, San Francisco, CA 94158"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Andrej","family":"Sali","sequence":"additional","affiliation":[{"name":"Departments of Biopharmaceutical Sciences and Pharmaceutical Chemistry, California Institute for Quantitative Biosciences, University of California, Mission Bay Byers Hall, 1700 Fourth Street, San Francisco, CA 94158"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Susan L.","family":"Hamilton","sequence":"additional","affiliation":[{"name":"Department of Molecular Physiology and Biophysics, Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Wah","family":"Chiu","sequence":"additional","affiliation":[{"name":"*National Center for Macromolecular Imaging, Verna and Marrs McLean Department of Biochemistry and Molecular Biology, and"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"341","published-online":{"date-parts":[[2008,7,15]]},"reference":[{"key":"e_1_3_3_1_2","doi-asserted-by":"publisher","DOI":"10.1038\/339439a0"},{"key":"e_1_3_3_2_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0021-9258(19)39968-5"},{"key":"e_1_3_3_3_2","doi-asserted-by":"crossref","first-page":"273","DOI":"10.1007\/978-1-4020-6191-2_10","volume-title":"Calcium Signaling and Disease","author":"Durham W","year":"2007","unstructured":"W Durham, X Wehrens, S Sood, SL Hamilton Calcium Signaling and Disease, eds E Carfoli, M Brini (Springer, New York), pp. 273\u2013321 (2007)."},{"key":"e_1_3_3_4_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.str.2005.06.005"},{"key":"e_1_3_3_5_2","doi-asserted-by":"publisher","DOI":"10.1038\/nsmb938"},{"key":"e_1_3_3_6_2","doi-asserted-by":"publisher","DOI":"10.1038\/nsb0696-547"},{"key":"e_1_3_3_7_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.jmb.2004.10.073"},{"key":"e_1_3_3_8_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0006-3495(99)77035-9"},{"key":"e_1_3_3_9_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.str.2006.11.008"},{"key":"e_1_3_3_10_2","doi-asserted-by":"publisher","DOI":"10.1038\/417515a"},{"key":"e_1_3_3_11_2","doi-asserted-by":"publisher","DOI":"10.1126\/science.1085028"},{"key":"e_1_3_3_12_2","doi-asserted-by":"publisher","DOI":"10.1038\/sj.emboj.7601828"},{"key":"e_1_3_3_13_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0092-8674(02)01227-8"},{"key":"e_1_3_3_14_2","doi-asserted-by":"publisher","DOI":"10.1038\/nn1411"},{"key":"e_1_3_3_15_2","doi-asserted-by":"publisher","DOI":"10.1038\/nature01922"},{"key":"e_1_3_3_16_2","doi-asserted-by":"publisher","DOI":"10.1093\/bioinformatics\/btg097"},{"key":"e_1_3_3_17_2","doi-asserted-by":"publisher","DOI":"10.1093\/bioinformatics\/btg124"},{"key":"e_1_3_3_18_2","doi-asserted-by":"publisher","DOI":"10.1093\/nar\/gki408"},{"key":"e_1_3_3_19_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.molcel.2004.11.047"},{"key":"e_1_3_3_20_2","doi-asserted-by":"publisher","DOI":"10.1038\/nature01268"},{"key":"e_1_3_3_21_2","doi-asserted-by":"publisher","DOI":"10.1006\/jmbi.1993.1626"},{"key":"e_1_3_3_22_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.jmb.2006.01.062"},{"key":"e_1_3_3_23_2","unstructured":"A Brunger X-PLOR: A system for X-ray crystallography and NMR.  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