中文摘要：

蛋白激酶Cα相互作用蛋白（PICK1）的PDZ结构域介导了PICK1和AMPAR的亚基GluR2的C末端结合,在GluR2下调引起兴奋性毒性而产生的多种神经性疾病中,PICK1的PDZ结构域是一个潜在的药物靶标.文章将重组质粒pET3a-pick1和pET-3C-GB-pdz转入E.coli BL21（DE3）,经IPTG诱导,在大肠杆菌中获得重组表达,目的蛋白经硫酸铵沉淀或Ni 2＋-NTA Sepharose 4Bcolumn亲和层析,再经Sephacryl S-200凝胶层析纯化得到了PICK1和GB-PDZ蛋白.利用荧光光谱法初步分析了款冬提取物与PICK1及其不同结构域的结合情况,结果表明款冬提取物与PICK1的结合位点位于PDZ结构域,款冬提取物能有效抑制PDZ结构域与GluR2的相互作用.

英文摘要：

Protein Interacting with Cα Kinase1（PICK1） contain PDZ domain,BAR domain and acidic amino region.PICK1 binds the AMPAR GluR2 subunit by its PDZ domain and is involved in AMPAR internalization and LTD.PICK1 PDZ domain was regarded as a potential drug target for neurological diseases.PICK1 and GB-PDZ,were overexpressed in Escherichia coli（DE3） and purified by（NH4）2SO4 fractionation or Ni2＋-NTA column and Sephacryl S-200 column.The effect of Tussilago farfara extract on the function of PICK1 was evaluated by fluorescence spectroscopy assay.The results indicated that there was some organic compounds in Tussilago farfara extract,which could bind the PDZ domain of PICK1,and Tussilago farfara extract inhibited the interaction between PDZ domain and GluR2.