The reciprocal nature of drug specificity and target specificity implies that the same is true for their respective promiscuities. Protein promiscuity has two broadly different types of footprint in drug design. The first is relaxed specificity of binding sites for substrates, inhibitors, effectors or cofactors. The second involves protein–protein interactions of regulatory processes such as signal transduction and transcription, and here protein intrinsic disorder plays an important role. Both viruses and host cells exploit intrinsic disorder for their survival, as do the design and discovery programs for antivirals. Drug action, strictly speaking, always relies upon promiscuous activity, with drug promiscuity enlarging its scope. Drug repurposing searches for additional promiscuity on the part of both the drug and the target in the host. Understanding the subtle nuances of these promiscuities is critical in the design of novel and more effective antivirals.

中文翻译：

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药物、宿主蛋白和病毒蛋白：它们的混杂如何影响抗病毒设计

药物特异性和靶点特异性的相互性质意味着它们各自的滥交也是如此。蛋白质混杂在药物设计中有两种截然不同的足迹。第一个是放松对底物、抑制剂、效应物或辅因子的结合位点的特异性。第二个涉及调节过程的蛋白质 - 蛋白质相互作用，例如信号转导和转录，在这里蛋白质内在紊乱起着重要作用。病毒和宿主细胞都利用内在的紊乱来生存，抗病毒药物的设计和发现程序也是如此。严格来说，毒品行为总是依赖于滥交活动，而毒品滥交则扩大了其范围。药物再利用在药物和宿主中的靶标方面寻找额外的滥交。