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However, the structural basis for\n                    <jats:italic>D-<\/jats:italic>\n                    stereoselectivity of a DNA polymerase has not been established, although two\n                    <jats:italic>L<\/jats:italic>\n                    -nucleoside analogs, lamivudine and emtricitabine, have been widely used as anti-HIV and anti-hepatitis B drugs. Here, we report ternary crystal structures of human DNA polymerase \u03bb in complex with DNA and\n                    <jats:italic>L<\/jats:italic>\n                    -deoxycytidine 5\u2032-triphosphate, or its analogs (the triphosphates of lamivudine and emtricitabine). These structures reveal that unlike a polymerase-bound\n                    <jats:italic>D<\/jats:italic>\n                    -nucleotide, an\n                    <jats:italic>L<\/jats:italic>\n                    -nucleotide initially interacts with an active site arginine residue through hydrogen bonds and then pairs with the templating nucleotide. Our work provides a structural basis for the\n                    <jats:italic>D-<\/jats:italic>\n                    stereoselectivity of a polymerase and valuable insight toward design of less toxic antiviral nucleoside analogs.\n                  <\/jats:p>","DOI":"10.1073\/pnas.1401286111","type":"journal-article","created":{"date-parts":[[2014,7,11]],"date-time":"2014-07-11T23:16:03Z","timestamp":1405120563000},"update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":20,"title":["Structural basis for the binding and incorporation of nucleotide analogs with\n                    <i>L<\/i>\n                    -stereochemistry by human DNA polymerase \u03bb"],"prefix":"10.1073","volume":"111","author":[{"given":"Rajan","family":"Vyas","sequence":"first","affiliation":[{"name":"Department of Chemistry and Biochemistry and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Walter J.","family":"Zahurancik","sequence":"additional","affiliation":[{"name":"Department of Chemistry and Biochemistry and"},{"name":"The Ohio State Biochemistry Program, The Ohio State University, Columbus, OH 43210"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Zucai","family":"Suo","sequence":"additional","affiliation":[{"name":"Department of Chemistry and Biochemistry and"},{"name":"The Ohio State Biochemistry Program, The Ohio State University, Columbus, OH 43210"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"341","published-online":{"date-parts":[[2014,7,11]]},"reference":[{"key":"e_1_3_4_1_2","doi-asserted-by":"crossref","first-page":"55","DOI":"10.1021\/bi982340r","article-title":"Mechanistic studies comparing the incorporation of (+) and (-) isomers of 3TCTP by HIV-1 reverse transcriptase","volume":"38","author":"Feng JY","year":"1999","unstructured":"JY Feng, KS Anderson, Mechanistic studies comparing the incorporation of (+) and (-) isomers of 3TCTP by HIV-1 reverse transcriptase. 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