Structures of HIV-1 RT–DNA complexes before and after incorporation of the anti-AIDS drug tenofovir
Tenofovir, also known as PMPA, R -9-(2-(phosphonomethoxypropyl)adenine, is a nucleotide reverse transcriptase (RT) inhibitor. We have determined the crystal structures of two related complexes of HIV-1 RT with template primer and tenofovir: (i) a ternary complex at a resolution of 3.0 Å of RT crossl...
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| Veröffentlicht in: | Nature structural & molecular biology 2004-05, Vol.11 (5), p.469-474 |
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| creator | Tuske, Steve Sarafianos, Stefan G Clark, Arthur D Ding, Jianping Naeger, Lisa K White, Kirsten L Miller, Michael D Gibbs, Craig S Boyer, Paul L Clark, Patrick Wang, Gang Gaffney, Barbara L Jones, Roger A Jerina, Donald M Hughes, Stephen H Arnold, Eddy |
| description | Tenofovir, also known as PMPA,
R
-9-(2-(phosphonomethoxypropyl)adenine, is a nucleotide reverse transcriptase (RT) inhibitor. We have determined the crystal structures of two related complexes of HIV-1 RT with template primer and tenofovir: (i) a ternary complex at a resolution of 3.0 Å of RT crosslinked to a dideoxy-terminated DNA with tenofovir-diphosphate bound as the incoming substrate; and (ii) a RT–DNA complex at a resolution of 3.1 Å with tenofovir at the 3′ primer terminus. The tenofovir nucleotide in the tenofovir-terminated structure seems to adopt multiple conformations. Some nucleoside reverse transcriptase inhibitors, including 3TC and AZT, have elements ('handles') that project beyond the corresponding elements on normal dNTPs (the 'substrate envelope'). HIV-1 RT resistance mechanisms to AZT and 3TC take advantage of these handles; tenofovir's structure lacks handles that could protrude through the substrate envelope to cause resistance. |
| doi_str_mv | 10.1038/nsmb760 |
| format | Article |
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R
-9-(2-(phosphonomethoxypropyl)adenine, is a nucleotide reverse transcriptase (RT) inhibitor. We have determined the crystal structures of two related complexes of HIV-1 RT with template primer and tenofovir: (i) a ternary complex at a resolution of 3.0 Å of RT crosslinked to a dideoxy-terminated DNA with tenofovir-diphosphate bound as the incoming substrate; and (ii) a RT–DNA complex at a resolution of 3.1 Å with tenofovir at the 3′ primer terminus. The tenofovir nucleotide in the tenofovir-terminated structure seems to adopt multiple conformations. Some nucleoside reverse transcriptase inhibitors, including 3TC and AZT, have elements ('handles') that project beyond the corresponding elements on normal dNTPs (the 'substrate envelope'). HIV-1 RT resistance mechanisms to AZT and 3TC take advantage of these handles; tenofovir's structure lacks handles that could protrude through the substrate envelope to cause resistance.</description><identifier>ISSN: 1545-9993</identifier><identifier>EISSN: 1545-9985</identifier><identifier>DOI: 10.1038/nsmb760</identifier><identifier>PMID: 15107837</identifier><language>eng</language><publisher>New York: Nature Publishing Group US</publisher><subject>Acquired immune deficiency syndrome ; Adenine - analogs & derivatives ; Adenine - chemistry ; AIDS ; Base Sequence ; Binding sites ; Biochemistry ; Biological Microscopy ; Biology ; Biomedical and Life Sciences ; Deoxyribonucleic acid ; DNA ; DNA Primers ; DNA, Viral - chemistry ; Drug resistance ; Enzymes ; Health aspects ; HIV ; HIV (Viruses) ; HIV Reverse Transcriptase - chemistry ; Human immunodeficiency virus ; Human immunodeficiency virus 1 ; Life Sciences ; Membrane Biology ; Models, Molecular ; Mutation ; Organophosphonates ; Organophosphorus Compounds - chemistry ; Physiological aspects ; Protein Structure ; Reverse transcriptase ; Reverse Transcriptase Inhibitors - chemistry ; Structure ; Substrates ; Tenofovir</subject><ispartof>Nature structural & molecular biology, 2004-05, Vol.11 (5), p.469-474</ispartof><rights>Springer Nature America, Inc. 2004</rights><rights>COPYRIGHT 2004 Nature Publishing Group</rights><rights>Copyright Nature Publishing Group May 2004</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c535t-c3a0ef05b050945d5ac3b538806564665730024a34cbdc9ec458cf93e7937ba83</citedby><cites>FETCH-LOGICAL-c535t-c3a0ef05b050945d5ac3b538806564665730024a34cbdc9ec458cf93e7937ba83</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1038/nsmb760$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1038/nsmb760$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27901,27902,41464,42533,51294</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15107837$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Tuske, Steve</creatorcontrib><creatorcontrib>Sarafianos, Stefan G</creatorcontrib><creatorcontrib>Clark, Arthur D</creatorcontrib><creatorcontrib>Ding, Jianping</creatorcontrib><creatorcontrib>Naeger, Lisa K</creatorcontrib><creatorcontrib>White, Kirsten L</creatorcontrib><creatorcontrib>Miller, Michael D</creatorcontrib><creatorcontrib>Gibbs, Craig S</creatorcontrib><creatorcontrib>Boyer, Paul L</creatorcontrib><creatorcontrib>Clark, Patrick</creatorcontrib><creatorcontrib>Wang, Gang</creatorcontrib><creatorcontrib>Gaffney, Barbara L</creatorcontrib><creatorcontrib>Jones, Roger A</creatorcontrib><creatorcontrib>Jerina, Donald M</creatorcontrib><creatorcontrib>Hughes, Stephen H</creatorcontrib><creatorcontrib>Arnold, Eddy</creatorcontrib><title>Structures of HIV-1 RT–DNA complexes before and after incorporation of the anti-AIDS drug tenofovir</title><title>Nature structural & molecular biology</title><addtitle>Nat Struct Mol Biol</addtitle><addtitle>Nat Struct Mol Biol</addtitle><description>Tenofovir, also known as PMPA,
R
-9-(2-(phosphonomethoxypropyl)adenine, is a nucleotide reverse transcriptase (RT) inhibitor. We have determined the crystal structures of two related complexes of HIV-1 RT with template primer and tenofovir: (i) a ternary complex at a resolution of 3.0 Å of RT crosslinked to a dideoxy-terminated DNA with tenofovir-diphosphate bound as the incoming substrate; and (ii) a RT–DNA complex at a resolution of 3.1 Å with tenofovir at the 3′ primer terminus. The tenofovir nucleotide in the tenofovir-terminated structure seems to adopt multiple conformations. Some nucleoside reverse transcriptase inhibitors, including 3TC and AZT, have elements ('handles') that project beyond the corresponding elements on normal dNTPs (the 'substrate envelope'). HIV-1 RT resistance mechanisms to AZT and 3TC take advantage of these handles; tenofovir's structure lacks handles that could protrude through the substrate envelope to cause resistance.</description><subject>Acquired immune deficiency syndrome</subject><subject>Adenine - analogs & derivatives</subject><subject>Adenine - chemistry</subject><subject>AIDS</subject><subject>Base Sequence</subject><subject>Binding sites</subject><subject>Biochemistry</subject><subject>Biological Microscopy</subject><subject>Biology</subject><subject>Biomedical and Life Sciences</subject><subject>Deoxyribonucleic acid</subject><subject>DNA</subject><subject>DNA Primers</subject><subject>DNA, Viral - chemistry</subject><subject>Drug resistance</subject><subject>Enzymes</subject><subject>Health aspects</subject><subject>HIV</subject><subject>HIV (Viruses)</subject><subject>HIV Reverse Transcriptase - chemistry</subject><subject>Human immunodeficiency virus</subject><subject>Human immunodeficiency virus 1</subject><subject>Life Sciences</subject><subject>Membrane Biology</subject><subject>Models, Molecular</subject><subject>Mutation</subject><subject>Organophosphonates</subject><subject>Organophosphorus Compounds - chemistry</subject><subject>Physiological aspects</subject><subject>Protein Structure</subject><subject>Reverse transcriptase</subject><subject>Reverse Transcriptase Inhibitors - 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R
-9-(2-(phosphonomethoxypropyl)adenine, is a nucleotide reverse transcriptase (RT) inhibitor. We have determined the crystal structures of two related complexes of HIV-1 RT with template primer and tenofovir: (i) a ternary complex at a resolution of 3.0 Å of RT crosslinked to a dideoxy-terminated DNA with tenofovir-diphosphate bound as the incoming substrate; and (ii) a RT–DNA complex at a resolution of 3.1 Å with tenofovir at the 3′ primer terminus. The tenofovir nucleotide in the tenofovir-terminated structure seems to adopt multiple conformations. Some nucleoside reverse transcriptase inhibitors, including 3TC and AZT, have elements ('handles') that project beyond the corresponding elements on normal dNTPs (the 'substrate envelope'). HIV-1 RT resistance mechanisms to AZT and 3TC take advantage of these handles; tenofovir's structure lacks handles that could protrude through the substrate envelope to cause resistance.</abstract><cop>New York</cop><pub>Nature Publishing Group US</pub><pmid>15107837</pmid><doi>10.1038/nsmb760</doi><tpages>6</tpages></addata></record> |
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| identifier | ISSN: 1545-9993 |
| ispartof | Nature structural & molecular biology, 2004-05, Vol.11 (5), p.469-474 |
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| source | MEDLINE; SpringerLink Journals (MCLS); Nature |
| subjects | Acquired immune deficiency syndrome Adenine - analogs & derivatives Adenine - chemistry AIDS Base Sequence Binding sites Biochemistry Biological Microscopy Biology Biomedical and Life Sciences Deoxyribonucleic acid DNA DNA Primers DNA, Viral - chemistry Drug resistance Enzymes Health aspects HIV HIV (Viruses) HIV Reverse Transcriptase - chemistry Human immunodeficiency virus Human immunodeficiency virus 1 Life Sciences Membrane Biology Models, Molecular Mutation Organophosphonates Organophosphorus Compounds - chemistry Physiological aspects Protein Structure Reverse transcriptase Reverse Transcriptase Inhibitors - chemistry Structure Substrates Tenofovir |
| title | Structures of HIV-1 RT–DNA complexes before and after incorporation of the anti-AIDS drug tenofovir |
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