1HNV
STRUCTURE OF HIV-1 RT(SLASH)TIBO R 86183 COMPLEX REVEALS SIMILARITY IN THE BINDING OF DIVERSE NONNUCLEOSIDE INHIBITORS
Summary for 1HNV
Entry DOI | 10.2210/pdb1hnv/pdb |
Descriptor | HIV-1 REVERSE TRANSCRIPTASE (SUBUNIT P66), HIV-1 REVERSE TRANSCRIPTASE (SUBUNIT P51), 5-CHLORO-8-METHYL-7-(3-METHYL-BUT-2-ENYL)-6,7,8,9-TETRAHYDRO-2H-2,7,9A-TRIAZA-BENZO[CD]AZULENE-1-THIONE (3 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 | 114507.88 |
Authors | Das, K.,Ding, J.,Arnold, E. (deposition date: 1995-03-30, release date: 1995-07-10, Last modification date: 2024-02-07) |
Primary citation | Ding, J.,Das, K.,Moereels, H.,Koymans, L.,Andries, K.,Janssen, P.A.,Hughes, S.H.,Arnold, E. Structure of HIV-1 RT/TIBO R 86183 complex reveals similarity in the binding of diverse nonnucleoside inhibitors. Nat.Struct.Biol., 2:407-415, 1995 Cited by PubMed Abstract: We report the structure of HIV-1 reverse transcriptase (RT) complexed with the nonnucleoside inhibitor TIBO R 86183 at 3.0 A resolution. Comparing this structure with those of complexes of HIV-1 RT/alpha-APA R 95845 and HIV-1 RT/nevirapine provides a basis for understanding the nature of nonnucleoside inhibitor binding, the structure of the binding site and the interactions between the bound inhibitors and surrounding amino acid residues as well as for understanding mechanisms of inhibition by and resistance to nonnucleoside inhibitors. All three inhibitors considered assume a similar butterfly-like shape and bind to HIV-1 RT in a very similar way. Important differences occur in the conformation of amino acid residues that form the binding pocket. PubMed: 7545077DOI: 10.1038/nsb0595-407 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3 Å) |
Structure validation
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