PDLIM2的PDZ结构域晶体结构及其与2-吗啉乙磺酸的相互作用研究

The Crystal Structure of PDZ Domain of PDLIM2 and Its Interaction with 2-Morpholineethanesulfonate

在之前的研究中曾发现PDLIM2蛋白能够通过其N端的PDZ结构域,与H5N1亚型流感病毒NS1蛋白的ESEV序列相互作用.解析了分辨率0.173 nm的PDLIM2的PDZ结构域晶体结构,发现2-吗啉乙磺酸(MES)分子能够与该PDZ结构域结合,并且占据PDZ结构域中与流感病毒NS1的ESEV序列相互作用的位点.进一步利用体外GST-pulldown实验证明,MES对于NS1与PDLIM2之间的相互作用具有一定的抑制效果.这一发现可能为开发与抗流感病毒相关的药物提供线索.

In our previous study,PDLIM2 protein can interact with the ESEV motif of the NS1 protein of H5 N1 influenza virus through its N-terminal PDZ domain.In this study,the crystal structure of the PDZ domain of PDLIM2 was determined at 0.173 nm resolution.In the structure,a 2-morpholineethanesulfonic acid(MES)molecule was found to bind to the PDZ domain and occupy its ESEV motif binding site.Further,using in vitro GST-pulldown experiment,MES can inhibit the interaction between NS1 and PDLIM2.This discovery may provide clues for anti-influenza virus drug development.