1rtj | pdb_00001rtj
MECHANISM OF INHIBITION OF HIV-1 REVERSE TRANSCRIPTASE BY NON-NUCLEOSIDE INHIBITORS
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Overview
The structure of unliganded HIV-1 reverse transcriptase has been, determined at 2.35 A resolution and refined to an R-factor of 0.219 (for, all data) with good stereochemistry. The unliganded structure was produced, by soaking out a weak binding non-nucleoside inhibitor, HEPT, from, pregrown crystals. Comparison with the structures of four different RT and, non-nucleoside inhibitor complexes reveals that only minor domain, rearrangements occur, but there is a significant repositioning of a, three-stranded beta-sheet in the p66 subunit (containing the catalytic, aspartic acid residues 110, 185 and 186) with respect to the rest of the, polymerase site. This suggests that NNIs inhibit RT by locking the, polymerase active site in an inactive conformation, reminiscent of the, conformation observed in the inactive p51 subunit.
About this Structure
1RTJ is a Protein complex structure of sequences from Human immunodeficiency virus 1 with CYA as ligand. Active as RNA-directed DNA polymerase, with EC number 2.7.7.49 Full crystallographic information is available from OCA.
Reference
Mechanism of inhibition of HIV-1 reverse transcriptase by non-nucleoside inhibitors., Esnouf R, Ren J, Ross C, Jones Y, Stammers D, Stuart D, Nat Struct Biol. 1995 Apr;2(4):303-8. PMID:7540935
Page seeded by OCA on Fri Feb 15 16:50:03 2008
