1REV

HIV-1 REVERSE TRANSCRIPTASE

Summary for 1REV

• Entry DOI: 10.2210/pdb1rev/pdb
• Descriptor: HIV-1 REVERSE TRANSCRIPTASE, MAGNESIUM ION, 4-CHLORO-8-METHYL-7-(3-METHYL-BUT-2-ENYL)-6,7,8,9-TETRAHYDRO-2H-2,7,9A-TRIAZA-BENZO[CD]AZULENE-1-THIONE, ... (5 entities in total)
• Functional Keywords: aids, polyprotein, hydrolase, aspartyl protease, endonuclease, nucleotidyltransferase, hiv-1 reverse transcriptase
• 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): P04585 P04585
• Total number of polymer chains: 2
• Total formula weight: 116340.17

Authors

Ren, J.,Esnouf, R.,Hopkins, A.,Ross, C.,Jones, Y.,Stammers, D.,Stuart, D. (deposition date: 1995-09-17, release date: 1996-10-14, Last modification date: 2024-10-23)

Primary citation

Ren, J.,Esnouf, R.,Hopkins, A.,Ross, C.,Jones, Y.,Stammers, D.,Stuart, D.
The structure of HIV-1 reverse transcriptase complexed with 9-chloro-TIBO: lessons for inhibitor design.
Structure, 3:915-926, 1995

PubMed Abstract: HIV reverse transcriptase (RT) is a key target of anti-AIDS therapies. Structural studies of HIV-1 RT, unliganded and complexed with different non-nucleoside inhibitors (NNIs), have pointed to a common mode of binding and inactivation through distortion of the polymerase catalytic site by NNIs containing two hinged rings. The mode of binding of the TIBO family of inhibitors is of interest because these compounds do not fit the two-hinged-ring model.

PubMed: 8535785
DOI: 10.1016/S0969-2126(01)00226-X

Experimental method

X-RAY DIFFRACTION (2.6 Å)