Result: Overall, these data suggest that the W252A and L303A mutations result in changes in the local conformation and intramolecular interactions of the surface-exposed residues of the HIV-1 thumb domain.
Discussion: Molecular dynamic simulations revealed that the W252A, L303A, and E298R mutations caused similar widespread structural changes and also caused a major r
Discussion: This raises the possibility that the larger structure-destabilizing effect of E298 may reduce the RT-eEF1A interaction by a mechanism similar to that of the W252A and L303A mutations described previously, and this mutation thereby acts via a mechanism different from that of the E300R mutation.
Specific Interaction between eEF1A and HIV RT Is Critical for HIV-1 Reverse Transcription and a Potential Anti-HIV Target.
Result: The W252A RT mutation affects late steps of reverse transcription and virus replication.
Result: The W252A RT mutation significantly reduced the association of RT with eEF1A in infected cells.
Result: Thermodynamic stability calculations using the empirical forcefield FoldX program show that the mutation W252A severely destabilizes structure in both individual s
Figure: (D) The RT activities of wild type and W252A RT mutated viruses were measured using a standard RT colorimetric assay and normalized to CA levels in each sample.
HIV mutation literature information.
PMID: 
2018
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