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• W2146241020 endingPage "724" @default.
• W2146241020 startingPage "704" @default.
• W2146241020 abstract "The emergence of drug resistance has devastating economic and social consequences, a testimonial of which is the rise and fall of inhibitors against the respiratory component cytochrome bc₁ complex, a time tested and highly effective target for disease control. Unfortunately, the mechanism of resistance is a multivariate problem, including primarily mutations in the gene of the cytochrome b subunit but also activation of alternative pathways of ubiquinol oxidation and pharmacokinetic effects. There is a considerable interest in designing new bc₁ inhibitors with novel modes of binding and lower propensity to induce the development of resistance. The accumulation of crystallographic data of bc₁ complexes with and without inhibitors bound provides the structural basis for rational drug design. In particular, the cytochrome b subunit offers two distinct active sites that can be targeted for inhibition - the quinol oxidation site and the quinone reduction site. This review brings together available structural information of inhibited bc₁ by various quinol oxidation- and reductionsite inhibitors, the inhibitor binding modes, conformational changes upon inhibitor binding of side chains in the active site and large scale domain movements of the iron-sulfur protein subunit. Structural data analysis provides a clear understanding of where and why existing inhibitors fail and points towards promising alternatives." @default.
• W2146241020 created "2016-06-24" @default.
• W2146241020 creator A5002229441 @default.
• W2146241020 creator A5053397364 @default.
• W2146241020 creator A5062624916 @default.
• W2146241020 date "2014-02-01" @default.
• W2146241020 modified "2023-09-25" @default.
• W2146241020 title "Structural Basis of Resistance to Anti-Cytochrome bc₁ Complex Inhibitors: Implication for Drug Improvement" @default.
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