Huang Ziwei
Department of Biochemistry, School of Molecular and Cellular Biology, University of Illinois at Urbana-Champaign, 61801, USA.
Mini Rev Med Chem. 2002 Aug;2(4):373-83. doi: 10.2174/1389557023405855.
Chemokine receptors are membrane proteins that play an important role in inflammation and the cellular entry of human immunodeficiency virus type I (HIV-1). Understanding the structure-function relationship of chemokine receptor-ligand interactions and developing novel strategies to control these interactions have important implications for therapeutic intervention of human diseases such as HIV-1 infection. This article reviews the work carried out in our laboratory in molecular modeling and site-directed mutagenesis of chemokine receptor-ligand interactions and chemical synthesis of chemokine-derived peptide agonists and antagonists. These studies demonstrate a paradigm for exploring and controlling membrane protein-protein interactions.
趋化因子受体是膜蛋白，在炎症反应以及I型人类免疫缺陷病毒（HIV-1）的细胞进入过程中发挥重要作用。了解趋化因子受体-配体相互作用的结构-功能关系并开发控制这些相互作用的新策略，对于诸如HIV-1感染等人类疾病的治疗干预具有重要意义。本文综述了我们实验室在趋化因子受体-配体相互作用的分子建模和定点诱变以及趋化因子衍生肽激动剂和拮抗剂的化学合成方面所开展的工作。这些研究展示了一种探索和控制膜蛋白-蛋白相互作用的范例。
