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1HNV

STRUCTURE OF HIV-1 RT(SLASH)TIBO R 86183 COMPLEX REVEALS SIMILARITY IN THE BINDING OF DIVERSE NONNUCLEOSIDE INHIBITORS

Summary for 1HNV
Entry DOI10.2210/pdb1hnv/pdb
DescriptorHIV-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 Keywordsnucleotidyltransferase
Biological sourceHuman immunodeficiency virus 1
More
Cellular locationMatrix 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 chains2
Total formula weight114507.88
Authors
Das, K.,Ding, J.,Arnold, E. (deposition date: 1995-03-30, release date: 1995-07-10, Last modification date: 2024-02-07)
Primary citationDing, 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: 7545077
DOI: 10.1038/nsb0595-407
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3 Å)
Structure validation

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数据于2025-06-25公开中

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