HLA-A*2402多肽复合物的两种构象——对Wolynes理论的补充  

Two conformations of pHLA-A*2402: a supplement to Wolynes’ theory

作　　者：刘传省[1,2] 施一[1] 高福[1] 

机构地区：[1]中国科学院微生物研究所中国科学院病原微生物与免疫学重点实验室,北京100101 [2]中国科学院研究生院,北京100049

出　　处：《生物工程学报》2012年第11期1370-1377,共8页Chinese Journal of Biotechnology

基　　金：国家自然科学基金(No.31030030)资助~~

摘　　要：Wolynes曾经提出,蛋白质的折叠沿着能量降低的方向进行,当达到一个能量的局部最低点,蛋白质就达到了一个相对稳定的状态。有些能量的局部最低点并非生物所需要,这样的能量最低点就成了能量陷阱。Wolynes的能量通道理论和自然选择学说很好地解释了蛋白质在生理状态下的高效折叠,而非掉入能量陷阱。至于存不存在可以逃脱自然选择的能量陷阱,一直没有明确的答案。文章发现HLA-A*2402多肽复合物(pHLA-A*2402)复性后至少存在两种不同的构象,并通过对其与TCR及CD8αα相互作用的研究,发现在pHLA-A*2402中存在两个可以逃脱自然选择的能量陷阱。Wolynes argued that the track of a protein＇s folding was directed by the tendency of lowering its energy, andthus when a local minimum of its energy was reached, a relatively stable conformation was formed. However not all of the local minimums will lead the protein to a biologically useful conformation, for those otherwise are called energy traps. Wolynes energy landscape theory and natural selection have well explained the high efficiency of protein folding in vivo, instead of being stuck in energy traps. As to whether a protein can assume different conformations with the same bioaetivity, there is no clear answer yet. In this paper, two conformational states of a pHLA-A＊2402 are discovered after refolding, and by studying their interactions with TCR and CD8act, two conformations ofpHLA-A＊2402 are confirmed of having escaped from natural selection.

关 键 词：蛋白折叠 能量陷阱 构象 自然选择 

分 类 号：Q51[生物学—生物化学]