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目的:研究人CCR5与CD4抗原和HIV-1包膜糖蛋白gp120的相互作用。方法:人CCR5受体的结构保守区由SYBYL软件中的Biopolymer模块建立,非保守区由LOOP SEARCH方法建立。将得到的结构模型与CD4抗原和gp120结合形成复合物。结果:人CCR5受体既可以与CD4抗原相互作用,也可以和gp120相互作用,其N-末端残基通过静电和氢键方式与CD4相互作用,并深埋在一个疏水中心里,被碱性基团包围。而且有7个氨基酸残基通过范德华作用、疏水性作用和氢键与6个gp120残基相互作用。结论:该模型将有助于设计作用更强的抗艾滋病药物。
AIM: To investigate the interaction of human CCR5 with CD4 antigen and HIV-1 envelope glycoprotein gp120. METHODS: The structural conserved region of human CCR5 receptor was established by the Biopolymer module in the SYBYL software and the non-conserved region was established by the LOOP SEARCH method. The resulting structural model is combined with CD4 antigen and gp120 to form a complex. Results: The human CCR5 receptor interacts with both the CD4 antigen and gp120, and its N-terminal residues interact with CD4 by electrostatic and hydrogen bonding and are buried deep in a hydrophobic center, Surrounded by groups. Moreover, seven amino acid residues interact with six gp120 residues through van der Waals’ action, hydrophobic interaction and hydrogen bonding. Conclusion: This model will help design stronger anti-AIDS drugs.