1T03
HIV-1 reverse transcriptase crosslinked to tenofovir terminated template-primer (complex P)
Summary for 1T03
| Entry DOI | 10.2210/pdb1t03/pdb |
| Related | 1N5Y 1N6Q 1T05 2HMI |
| Descriptor | Synthetic oligonucleotide template, Synthetic oligonucleotide primer, POL polyprotein, ... (7 entities in total) |
| Functional Keywords | hiv-1 rt, tenofovir, rt-dna complex, transferase-antibody-dna complex, transferase/antibody/dna |
| Biological source | Human immunodeficiency virus 1 More |
| Cellular location | Matrix protein p17: Virion (Potential). Capsid protein p24: Virion (Potential). Nucleocapsid protein p7: Virion (Potential). Reverse transcriptase/ribonuclease H: Virion (Potential). Integrase: Virion (Potential): P03366 P03366 |
| Total number of polymer chains | 6 |
| Total formula weight | 177530.69 |
| Authors | Tuske, S.,Sarafianos, S.G.,Ding, J.,Arnold, E. (deposition date: 2004-04-07, release date: 2004-05-11, Last modification date: 2024-11-13) |
| Primary citation | Tuske, S.,Sarafianos, S.G.,Clark Jr., A.D.,Ding, J.,Naeger, L.K.,White, K.L.,Miller, M.D.,Gibbs, C.S.,Boyer, P.L.,Clark, P.,Wang, G.,Gaffney, B.L.,Jones, R.A.,Jerina, D.M.,Hughes, S.H.,Arnold, E. Structure of HIV-1 RT-DNA complexes before and after incorporation of the anti-AIDS drug tenofovir Nat.Struct.Mol.Biol., 11:469-474, 2004 Cited by PubMed Abstract: 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 A 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 A 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. PubMed: 15107837DOI: 10.1038/nsmb760 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.1 Å) |
Structure validation
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