1DLO
HUMAN IMMUNODEFICIENCY VIRUS TYPE 1
Summary for 1DLO
Entry DOI | 10.2210/pdb1dlo/pdb |
Descriptor | HUMAN IMMUNODEFICIENCY VIRUS TYPE 1 REVERSE TRANSCRIPTASE (2 entities in total) |
Functional Keywords | nucleotidyltransferase |
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 | 2 |
Total formula weight | 113899.63 |
Authors | Hsiou, Y.,Ding, J.,Das, K.,Hughes, S.,Arnold, E. (deposition date: 1996-04-17, release date: 1996-08-01, Last modification date: 2024-02-07) |
Primary citation | Hsiou, Y.,Ding, J.,Das, K.,Clark Jr., A.D.,Hughes, S.H.,Arnold, E. Structure of unliganded HIV-1 reverse transcriptase at 2.7 A resolution: implications of conformational changes for polymerization and inhibition mechanisms. Structure, 4:853-860, 1996 Cited by PubMed Abstract: HIV-1 reverse transcriptase (RT) is a major target for anti-HIV drugs. A considerable amount of information about the structure of RT is available, both unliganded and in complex with template-primer or non-nucleoside RT inhibitors (NNRTIs). But significant conformational differences in the p66 polymerase domain among the unliganded structures have complicated the interpretation of these data, leading to different proposals for the mechanisms of polymerization and inhibition. PubMed: 8805568DOI: 10.1016/S0969-2126(96)00091-3 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
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