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1TL3

Crystal structure of hiv-1 reverse transcriptase in complex with gw450557

Summary for 1TL3
Entry DOI10.2210/pdb1tl3/pdb
DescriptorPol polyprotein, Reverse transcriptase, Chain A, Pol polyprotein, Reverse transcriptase, Chain B, PHOSPHATE ION, ... (4 entities in total)
Functional Keywordshiv-1 reverse transcriptase, aids, nnrti, gw450557, drug design, transferase
Biological sourceHuman immunodeficiency virus 1
More
Cellular locationGag-Pol polyprotein: Host cell membrane; Lipid-anchor . Matrix protein p17: Virion membrane; Lipid- anchor . Capsid protein p24: Virion . Nucleocapsid protein p7: Virion . Reverse transcriptase/ribonuclease H: Virion . Integrase: Virion : P04585 P04585
Total number of polymer chains2
Total formula weight116598.74
Authors
Hopkins, A.L.,Ren, J.,Stuart, D.I.,Stammers, D.K. (deposition date: 2004-06-09, release date: 2004-12-07, Last modification date: 2024-10-30)
Primary citationHopkins, A.L.,Ren, J.,Milton, J.,Hazen, R.J.,Chan, J.H.,Stuart, D.I.,Stammers, D.K.
Design of non-nucleoside inhibitors of HIV-1 reverse transcriptase with improved drug resistance properties. 1.
J.Med.Chem., 47:5912-5922, 2004
Cited by
PubMed Abstract: We have used a structure-based approach to design a novel series of non-nucleoside inhibitors of HIV-1 RT (NNRTIs). Detailed analysis of a wide range of crystal structures of HIV-1 RT-NNRTI complexes together with data on drug resistance mutations has identified factors important for tight binding of inhibitors and resilience to mutations. Using this approach we have designed and synthesized a novel series of quinolone NNRTIs. Crystal structure analysis of four of these compounds in complexes with HIV-1 RT confirms the predicted binding modes. Members of this quinolone series retain high activity against the important resistance mutations in RT at Tyr181Cys and Leu100Ile.
PubMed: 15537346
DOI: 10.1021/jm040071z
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.8 Å)
Structure validation

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