{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,26]],"date-time":"2026-09-26T12:32:24Z","timestamp":1790425944691,"version":"4.1.0"},"reference-count":40,"publisher":"National Academy of Sciences","issue":"20","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2010,5,18]]},"abstract":"<jats:p>\n                    The C-terminal cytoplasmic tail of polycystin-2 (PC2\/TRPP2), a Ca\n                    <jats:sup>2+<\/jats:sup>\n                    -permeable channel, is frequently mutated or truncated in autosomal dominant polycystic kidney disease. We have previously shown that this tail consists of three functional regions: an EF-hand domain (PC2-EF, 720\u2013797), a flexible linker (798\u2013827), and an oligomeric coiled coil domain (828\u2013895). We found that PC2-EF binds Ca\n                    <jats:sup>2+<\/jats:sup>\n                    at a single site and undergoes Ca\n                    <jats:sup>2+<\/jats:sup>\n                    -dependent conformational changes, suggesting it is an essential element of Ca\n                    <jats:sup>2+<\/jats:sup>\n                    -sensitive regulation of PC2 activity. Here we describe the NMR structure and dynamics of Ca\n                    <jats:sup>2+<\/jats:sup>\n                    -bound PC2-EF. Human PC2-EF contains a divergent non-Ca\n                    <jats:sup>2+<\/jats:sup>\n                    -binding helix-loop-helix (HLH) motif packed against a canonical Ca\n                    <jats:sup>2+<\/jats:sup>\n                    -binding EF-hand motif. This HLH motif may have evolved from a canonical EF-hand found in invertebrate PC2 homologs. Temperature-dependent steady-state NOE experiments and NMR\n                    <jats:italic>R<\/jats:italic>\n                    <jats:sub>1<\/jats:sub>\n                    and\n                    <jats:italic>R<\/jats:italic>\n                    <jats:sub>2<\/jats:sub>\n                    relaxation rates correlate with increased molecular motion in the EF-hand, possibly due to exchange between apo and Ca\n                    <jats:sup>2+<\/jats:sup>\n                    -bound states, consistent with a role for PC2-EF as a Ca\n                    <jats:sup>2+<\/jats:sup>\n                    -sensitive regulator. Structure-based sequence conservation analysis reveals a conserved hydrophobic surface in the same region, which may mediate Ca\n                    <jats:sup>2+<\/jats:sup>\n                    -dependent protein interactions. We propose that Ca\n                    <jats:sup>2+<\/jats:sup>\n                    -sensing by PC2-EF is responsible for the cooperative nature of PC2 channel activation and inhibition. Based on our results, we present a mechanism of regulation of the Ca\n                    <jats:sup>2+<\/jats:sup>\n                    dependence of PC2 channel activity by PC2-EF.\n                  <\/jats:p>","DOI":"10.1073\/pnas.0912295107","type":"journal-article","created":{"date-parts":[[2010,5,3]],"date-time":"2010-05-03T22:02:58Z","timestamp":1272924178000},"page":"9176-9181","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":72,"title":["Structure of the EF-hand domain of polycystin-2 suggests a mechanism for Ca\n                    <sup>2+<\/sup>\n                    -dependent regulation of polycystin-2 channel activity"],"prefix":"10.1073","volume":"107","author":[{"given":"Edward T.","family":"Petri","sequence":"first","affiliation":[{"name":"Department of Pharmacology, Yale University School of Medicine, 333 Cedar Street, New Haven, CT 06520;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Andjelka","family":"\u0106eli\u0107","sequence":"additional","affiliation":[{"name":"Department of Pharmacology, Yale University School of Medicine, 333 Cedar Street, New Haven, CT 06520;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Scott D.","family":"Kennedy","sequence":"additional","affiliation":[{"name":"Laboratory Medicine, Yale University School of Medicine, 333 Cedar Street, New Haven, CT 06520."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Barbara E.","family":"Ehrlich","sequence":"additional","affiliation":[{"name":"Department of Pharmacology, Yale University School of Medicine, 333 Cedar Street, New Haven, CT 06520;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Titus J.","family":"Boggon","sequence":"additional","affiliation":[{"name":"Department of Pharmacology, Yale University School of Medicine, 333 Cedar Street, New Haven, CT 06520;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Michael E.","family":"Hodsdon","sequence":"additional","affiliation":[{"name":"University of Rochester School of Medicine, Rochester, NY 14620; and"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"341","published-online":{"date-parts":[[2010,5,3]]},"reference":[{"key":"e_1_3_4_1_2","doi-asserted-by":"crossref","first-page":"177","DOI":"10.1016\/S0092-8674(00)81570-6","article-title":"Somatic inactivation of Pkd2 results in polycystic kidney disease","volume":"93","author":"Wu G","year":"1998","unstructured":"G Wu, et al., Somatic inactivation of Pkd2 results in polycystic kidney disease. Cell 93, 177\u2013188 (1998).","journal-title":"Cell"},{"key":"e_1_3_4_2_2","doi-asserted-by":"crossref","first-page":"149","DOI":"10.1038\/ki.2009.128","article-title":"Autosomal dominant polycystic kidney disease: The last 3\u00a0years","volume":"76","author":"Torres VE","year":"2009","unstructured":"VE Torres, PC Harris, Autosomal dominant polycystic kidney disease: The last 3\u00a0years. Kidney Int 76, 149\u2013168 (2009).","journal-title":"Kidney Int"},{"key":"e_1_3_4_3_2","doi-asserted-by":"crossref","first-page":"129","DOI":"10.1038\/ng1076","article-title":"Polycystins 1 and 2 mediate mechanosensation in the primary cilium of kidney cells","volume":"33","author":"Nauli SM","year":"2003","unstructured":"SM Nauli, et al., Polycystins 1 and 2 mediate mechanosensation in the primary cilium of kidney cells. Nat Genet 33, 129\u2013137 (2003).","journal-title":"Nat Genet"},{"key":"e_1_3_4_4_2","doi-asserted-by":"crossref","first-page":"191","DOI":"10.1038\/ncb754","article-title":"Polycystin-2 is an intracellular calcium release channel","volume":"4","author":"Koulen P","year":"2002","unstructured":"P Koulen, et al., Polycystin-2 is an intracellular calcium release channel. Nat Cell Biol 4, 191\u2013197 (2002).","journal-title":"Nat Cell Biol"},{"key":"e_1_3_4_5_2","doi-asserted-by":"crossref","first-page":"179","DOI":"10.1038\/ng0697-179","article-title":"PKD1 interacts with PKD2 through a probable coiled-coil domain","volume":"16","author":"Qian F","year":"1997","unstructured":"F Qian, et al., PKD1 interacts with PKD2 through a probable coiled-coil domain. 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J Biol Chem 283, 28305\u201312 (2008).","journal-title":"J Biol Chem"},{"key":"e_1_3_4_8_2","doi-asserted-by":"crossref","first-page":"11558","DOI":"10.1073\/pnas.0903684106","article-title":"Structural and molecular basis of the assembly of the TRPP2\/PKD1 complex","volume":"106","author":"Yu Y","year":"2009","unstructured":"Y Yu, et al., Structural and molecular basis of the assembly of the TRPP2\/PKD1 complex. Proc Natl Acad Sci USA 106, 11558\u201311563 (2009).","journal-title":"Proc Natl Acad Sci USA"},{"key":"e_1_3_4_9_2","doi-asserted-by":"crossref","first-page":"666","DOI":"10.1002\/mus.21155","article-title":"New mutation of the Na channel in the severe form of potassium-aggravated myotonia","volume":"39","author":"Kubota T","year":"2009","unstructured":"T Kubota, et al., New mutation of the Na channel in the severe form of potassium-aggravated myotonia. 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J Biol Chem 279, 19987\u201319995 (2004).","journal-title":"J Biol Chem"},{"key":"e_1_3_4_15_2","doi-asserted-by":"crossref","first-page":"209","DOI":"10.1016\/S0022-2836(02)00241-3","article-title":"Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA","volume":"319","author":"Herrmann T","year":"2002","unstructured":"T Herrmann, P Guntert, K Wuthrich, Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA. J Mol Biol 319, 209\u2013227 (2002).","journal-title":"J Mol Biol"},{"key":"e_1_3_4_16_2","doi-asserted-by":"crossref","first-page":"65","DOI":"10.1016\/S1090-7807(02)00014-9","article-title":"The Xplor-NIH NMR molecular structure determination package","volume":"160","author":"Schwieters CD","year":"2003","unstructured":"CD Schwieters, et al., The Xplor-NIH NMR molecular structure determination package. 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