| Literature DB >> 30475264 |
Kyle J Hill1,2,3, Leonard C Rogers1,3,4, Duncan T Njenda5, Donald H Burke1,2, Stefan G Sarafianos6, Anders Sönnerborg5,7, Ujjwal Neogi5, Kamalendra Singh1,2,5.
Abstract
: The oligomerization of HIV-1 integrase onto DNA is not well understood. Here we show that HIV-1 integrase binds the DNA in biphasic (high-affinity and low-affinity) modes. For HIV-1 subtype B, the high-affinity mode is ∼100-fold greater than the low-affinity mode (Kd.DNA = 37 and 3400 nmol/l, respectively). The Kd.DNA values of patient-derived integrases containing subtype-specific polymorphisms were affected two- to four-fold, suggesting that polymorphisms may have an influence on effective-concentrations of inhibitors, as these inhibitors preferably bind to integrase-DNA complex.Entities:
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Year: 2019 PMID: 30475264 PMCID: PMC6472922 DOI: 10.1097/QAD.0000000000002078
Source DB: PubMed Journal: AIDS ISSN: 0269-9370 Impact factor: 4.177