Hydrophobic Core Flexibility Modulates Enzyme Activity in HIV-1 Protease
نویسندگان
چکیده
منابع مشابه
Targeting structural flexibility in HIV-1 protease inhibitor binding.
HIV-1 protease remains an important anti-AIDS drug target. Although it has been known that ligand binding induces large conformational changes in the protease, the dynamic aspects of binding have been largely ignored. Several computational models describing protease dynamics have been reported recently. These have reproduced experimental observations, and have also explained how ligands gain ac...
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The flexibility and stability of both monomeric and dimeric HIV-1 PR were explored by 100 ns implicit solvent molecular dynamics simulation at 350 K with the aim to correlate the monomer stability with the dimerization mechanism. The principal component analysis (PCA) was applied to visualize the available regions in the conformational space of the two HIV-1 PR forms, to compare their structura...
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Inhibitors of the protease of HIV-1 have been used successfully for the treatment of HIV-1-infected patients and AIDS disease. We tested whether these protease inhibitory drugs exerted effects in addition to their antiviral activity. Here, we show in mice infected with lymphocytic choriomeningitis virus and treated with the HIV-1 protease inhibitor ritonavir a marked inhibition of antiviral cyt...
متن کاملHIV-1 protease inhibitors.
Treatment of human immunodeficiency virus type 1 (HIV-1) infection with regimens that include protease inhibitors (PIs) has contributed to marked improvements in HIV-related disease progression and mortality. Five PIs are approved by the US Food and Drug Administration and have potent activity in vitro. PIs with 2 nucleoside analogue reverse transcriptase inhibitors have demonstrated prolonged ...
متن کاملCollective motions in HIV-1 reverse transcriptase: examination of flexibility and enzyme function.
In order to study the inferences of structure for mechanism, the collective motions of the retroviral reverse transcriptase HIV-1 RT (RT) are examined using the Gaussian network model (GNM) of proteins. This model is particularly suitable for elucidating the global dynamic characteristics of large proteins such as the presently investigated heterodimeric RT comprising a total of 982 residues. L...
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ژورنال
عنوان ژورنال: Journal of the American Chemical Society
سال: 2012
ISSN: 0002-7863,1520-5126
DOI: 10.1021/ja2095766