Mutational analysis of two conserved sequence motifs in HIV-1 reverse transcriptase
| Autor: | S. D. Kemp, Vanita Parmar, Brendan Larder, Denise M. Lowe |
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| Rok vydání: | 1991 |
| Předmět: |
Phosphonoacetic Acid
Reverse transcriptase (HIV-1) DNA Mutational Analysis Molecular Sequence Data Mutant Biophysics Mutagenesis (molecular biology technique) In Vitro Techniques Biology medicine.disease_cause Biochemistry Conserved sequence Serine Structure-Activity Relationship Structural Biology Genetics medicine Thymine Nucleotides Conserved sequence motif Amino Acid Sequence Asparagine Site-directed mutagenesis Molecular Biology Mutation RNA-Directed DNA Polymerase Cell Biology Molecular biology Recombinant Proteins Reverse transcriptase Enzyme inhibition Kinetics HIV-1 Reverse Transcriptase Inhibitors Zidovudine Dideoxynucleotides Foscarnet |
| Zdroj: | FEBS Letters. 282:231-234 |
| ISSN: | 0014-5793 |
| Popis: | Two conserved sequence motifs, occurring in HIV-1 reverse transcriptase at residues 110–116 and 183–190, have been studied using site-directed mutagenesis of the cloned gene. In particular, aspariates at positions 185 and 186 have each been mutated to either asparagine or glutamate. The resulting mutant proteins were catalytically inactive but still able to bind the template-primer complex, poly rA-oligo dT. Other mutations in these regions results in reduced reverse transcriptase activity but the mutation of tyrosine-183 to serine caused a significant increase in the Km for dTTP and the Km for inhibition by 3′-azi-Jothymidine-triphosphate, 2′3′-dideoxythymidine-triphosphate and phosphonoformic acid. |
| Databáze: | OpenAIRE |
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