{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,7]],"date-time":"2026-07-07T11:19:41Z","timestamp":1783423181356,"version":"3.54.6"},"reference-count":62,"publisher":"Oxford University Press (OUP)","issue":"3","license":[{"start":{"date-parts":[[2026,6,19]],"date-time":"2026-06-19T00:00:00Z","timestamp":1781827200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"Center for Bio-Molecular Structure"},{"DOI":"10.13039\/100000002","name":"US National Institutes of Health","doi-asserted-by":"publisher","award":["P30 GM133893"],"award-info":[{"award-number":["P30 GM133893"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"NIH","doi-asserted-by":"publisher","award":["NIGMS R35-GM118047"],"award-info":[{"award-number":["NIGMS R35-GM118047"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000060","name":"NIAID","doi-asserted-by":"publisher","award":["U19-AI171954"],"award-info":[{"award-number":["U19-AI171954"]}],"id":[{"id":"10.13039\/100000060","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2026,7,6]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>Three-prime Repair EXonuclease 1 (TREX1) is a 3\u2032-to-5\u2032 exonuclease that degrades cytoplasmic DNA to prevent aberrant innate immune and inflammatory responses. Loss of TREX1 function results in the accumulation of cytosolic DNA and autoimmune disorders in humans, whereas in cancer cells, TREX1 inhibition can promote antitumor immunity triggered by tumor-derived cytoplasmic DNA. Here, we show selective inhibition of human TREX1 (hTREX1) by small molecule inhibitors and reveal their mechanism of target engagement by X-ray crystallography. The structures show that these inhibitors competitively block the binding of the 3\u2032-terminal nucleotide of DNA substrates and make a hydrogen bond with a conserved Glu residue in the active site. Furthermore, binding of the inhibitors stabilizes Tyr129 of hTREX1 in an alternative conformation incompatible with DNA binding, generating a deep hydrophobic pocket that accommodates a key aromatic moiety of the inhibitors. The structural observations provide the basis for high selectivity of these inhibitors for hTREX1 over the closely related hTREX2 or other viral DEDDh-family nucleases. Our studies demonstrate that the conformational flexibility of the hTREX1 active site plays a crucial role in its selective inhibition, informing future design of hTREX1-selective ligands through this structural framework.<\/jats:p>","DOI":"10.1093\/narmme\/ugag033","type":"journal-article","created":{"date-parts":[[2026,6,19]],"date-time":"2026-06-19T11:51:41Z","timestamp":1781869901000},"source":"Crossref","is-referenced-by-count":0,"title":["Selective targeting of human TREX1 exonuclease by small molecule inhibitors is mediated by a conformational switch"],"prefix":"10.1093","volume":"3","author":[{"given":"Patricia C","family":"Hernandez","sequence":"first","affiliation":[{"name":"Department of Biochemistry, Molecular Biology and Biophysics, University of Minnesota , Minneapolis, MN 55455 ,","place":["United States"]},{"name":"Institute for Molecular Virology, University of Minnesota , Minneapolis, MN 55455 ,","place":["United States"]},{"name":"Masonic Cancer Center, University of Minnesota , Minneapolis, MN 55455 ,","place":["United States"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rahul Dadabhau","family":"Kardile","sequence":"additional","affiliation":[{"name":"Institute for Molecular Virology, University of Minnesota , Minneapolis, MN 55455 ,","place":["United States"]},{"name":"Masonic Cancer Center, University of Minnesota , Minneapolis, MN 55455 ,","place":["United States"]},{"name":"Department of Medicinal Chemistry, University of Minnesota , Minneapolis, MN 55455 ,","place":["United States"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ke","family":"Shi","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, Molecular Biology and Biophysics, University of Minnesota , Minneapolis, MN 55455 ,","place":["United States"]},{"name":"Institute for Molecular Virology, University of Minnesota , Minneapolis, MN 55455 ,","place":["United States"]},{"name":"Masonic Cancer Center, University of Minnesota , Minneapolis, MN 55455 ,","place":["United States"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nicholas H","family":"Moeller","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, Molecular Biology and Biophysics, University of Minnesota , Minneapolis, MN 55455 ,","place":["United States"]},{"name":"Institute for Molecular Virology, University of Minnesota , Minneapolis, MN 55455 ,","place":["United States"]},{"name":"Masonic Cancer Center, University of Minnesota , Minneapolis, MN 55455 ,","place":["United States"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Joseph\u00a0A","family":"Rollie","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, Molecular Biology and Biophysics, University of Minnesota , Minneapolis, MN 55455 ,","place":["United States"]},{"name":"Institute for Molecular Virology, University of Minnesota , Minneapolis, MN 55455 ,","place":["United States"]},{"name":"Masonic Cancer Center, University of Minnesota , Minneapolis, MN 55455 ,","place":["United States"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-5950-931X","authenticated-orcid":false,"given":"Daniel A","family":"Harki","sequence":"additional","affiliation":[{"name":"Institute for Molecular Virology, University of Minnesota , Minneapolis, MN 55455 ,","place":["United States"]},{"name":"Masonic Cancer Center, University of Minnesota , Minneapolis, MN 55455 ,","place":["United States"]},{"name":"Department of Medicinal Chemistry, University of Minnesota , Minneapolis, MN 55455 ,","place":["United States"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-7508-6230","authenticated-orcid":false,"given":"Hideki","family":"Aihara","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, Molecular Biology and Biophysics, University of Minnesota , Minneapolis, MN 55455 ,","place":["United States"]},{"name":"Institute for Molecular Virology, University of Minnesota , Minneapolis, MN 55455 ,","place":["United States"]},{"name":"Masonic Cancer Center, University of Minnesota , Minneapolis, MN 55455 ,","place":["United States"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"286","published-online":{"date-parts":[[2026,6,19]]},"reference":[{"key":"2026070707064195200_B1","doi-asserted-by":"publisher","first-page":"463","DOI":"10.1016\/j.immuni.2015.07.022","article-title":"Cytosolic nuclease TREX1 regulates oligosaccharyltransferase activity independent of nuclease activity to suppress immune activation","volume":"43","author":"Hasan","year":"2015","journal-title":"Immunity"},{"key":"2026070707064195200_B2","doi-asserted-by":"publisher","first-page":"587","DOI":"10.1016\/j.cell.2008.06.032","article-title":"Trex1 prevents cell-intrinsic initiation of 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Identification of a new active histidine conserved in DEDDh exonucleases","volume":"17","author":"Brucet","year":"2008","journal-title":"Protein Sci"},{"key":"2026070707064195200_B5","doi-asserted-by":"publisher","first-page":"14547","DOI":"10.1074\/jbc.M700236200","article-title":"Structure of the dimeric exonuclease TREX1 in complex with DNA displays a proline-rich binding site for WW Domains","volume":"282","author":"Brucet","year":"2007","journal-title":"J Biol Chem"},{"key":"2026070707064195200_B6","doi-asserted-by":"crossref","first-page":"10537","DOI":"10.1074\/jbc.M700039200","article-title":"The crystal structure of TREX1 explains the 3\u2032 nucleotide specificity and reveals a polyproline II helix for protein partnering","volume":"282","author":"de\u00a0Silva","year":"2007","journal-title":"J Biol Chem"},{"key":"2026070707064195200_B7","doi-asserted-by":"crossref","first-page":"19655","DOI":"10.1074\/jbc.274.28.19655","article-title":"Identification and expression of the 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