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Cooper Medical Research Foundation","doi-asserted-by":"publisher","award":["PG2019396"],"award-info":[{"award-number":["PG2019396"]}],"id":[{"id":"10.13039\/501100001061","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000925","name":"National Health and Medical Research Council","doi-asserted-by":"publisher","award":["APP1072113"],"award-info":[{"award-number":["APP1072113"]}],"id":[{"id":"10.13039\/501100000925","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elifesciences.org"],"crossmark-restriction":false},"short-container-title":[],"accepted":{"date-parts":[[2022,7,19]]},"abstract":"<jats:p>\n                    Low voltage-activated calcium currents are mediated by T-type calcium channels Ca\n                    <jats:sub>V<\/jats:sub>\n                    3.1, Ca\n                    <jats:sub>V<\/jats:sub>\n                    3.2, and Ca\n                    <jats:sub>V<\/jats:sub>\n                    3.3, which modulate a variety of physiological processes including sleep, cardiac pace-making, pain, and epilepsy. Ca\n                    <jats:sub>V<\/jats:sub>\n                    3 isoforms\u2019 biophysical properties, overlapping expression, and lack of subtype-selective pharmacology hinder the determination of their specific physiological roles in health and disease. We have identified \u03bc-theraphotoxin Pn3a as the first subtype-selective spider venom peptide inhibitor of Ca\n                    <jats:sub>V<\/jats:sub>\n                    3.3, with &gt;100-fold lower potency against the other T-type isoforms. Pn3a modifies Ca\n                    <jats:sub>V<\/jats:sub>\n                    3.3 gating through a depolarizing shift in the voltage dependence of activation thus decreasing Ca\n                    <jats:sub>V<\/jats:sub>\n                    3.3-mediated currents in the normal range of activation potentials. Paddle chimeras of K\n                    <jats:sub>V<\/jats:sub>\n                    1.7 channels bearing voltage sensor sequences from all four Ca\n                    <jats:sub>V<\/jats:sub>\n                    3.3 domains revealed preferential binding of Pn3a to the S3-S4 region of domain II (Ca\n                    <jats:sub>V<\/jats:sub>\n                    3.3\n                    <jats:sup>DII<\/jats:sup>\n                    ). This novel T-type channel pharmacological site was explored through computational docking simulations of Pn3a, site-directed mutagenesis, and full domain II swaps between Ca\n                    <jats:sub>V<\/jats:sub>\n                    3 channels highlighting it as a subtype-specific pharmacophore. This research expands our understanding of T-type calcium channel pharmacology and supports the suitability of Pn3a as a molecular tool in the study of the physiological roles of Ca\n                    <jats:sub>V<\/jats:sub>\n                    3.3 channels.\n                  <\/jats:p>","DOI":"10.7554\/elife.74040","type":"journal-article","created":{"date-parts":[[2022,7,20]],"date-time":"2022-07-20T08:00:32Z","timestamp":1658304032000},"update-policy":"https:\/\/doi.org\/10.7554\/elife.74040","source":"Crossref","is-referenced-by-count":6,"title":["\u00b5-Theraphotoxin Pn3a inhibition of CaV3.3 channels reveals a novel isoform-selective drug binding site"],"prefix":"10.7554","volume":"11","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-2546-7913","authenticated-orcid":true,"given":"Jeffrey R","family":"McArthur","sequence":"first","affiliation":[{"id":[{"id":"https:\/\/ror.org\/00jtmb277","id-type":"ROR","asserted-by":"publisher"}],"name":"Illawarra Health and Medical 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