Epitope mapping and conformational analysis of SV40 T-antigen deletion mutants.
Epitope mapping and conformational analysis of SV40 T-antigen deletion mutants.
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SV40 T 抗原缺失突变体的表位作图和构象分析。
DOI：
10.1016/0042-6822(92)90606-p
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发表时间：
1992
期刊：
影响因子：
3.7
通讯作者：
Butel,JS
中科院分区：
文献类型：
--
作者：
Sawai,ET;Butel,JS
SV 40 T抗原缺失突变体在BALB/c 3 T3 E细胞中稳定表达，并在免疫沉淀试验中使用T抗原特异性单克隆抗体进行表征。由抗体PAb 602识别的表位缩窄至T-抗原残基230-362。共沉淀结果与T抗原氨基酸347和517之间的p53结合区相容。基于抗体结合和与p53的结合，T抗原的氨基末端缺失（1-108或98-229）似乎对分子远端区域的构象具有显著影响。
Deletion mutants of SV40 T-antigen were stably expressed in BALB/c 3T3E cells and characterized in immunoprecipitation assays using T-antigen-specific monoclonal antibodies. The epitope recognized by antibody PAb602 was narrowed to T-antigen residues 230–362. Coprecipitation results were compatible with a p53-binding region between T-antigen amino acids 347 and 517. Amino terminal deletions (1–108 or 98–229) of T-antigen appeared to have pronounced effects on the conformation of distal regions of the molecule, based both on antibody binding and on association with p53.