摘要
采用密度泛函活性理论研究了以锌指蛋白为基础建立的3种锌指模型,MS4-xNx(M为二价金属离子Mg,Ca,Sc,Ti,V,Cr,Mn,Fe,Co,Ni,Cu,Zn;S和N分别代表组氨酸和半胱氨酸残基;x=0,1,2),并探讨了其金属结合特异性.结果表明,当锌离子参与键合时,体系既表现出最大稳定性,同时又显示出最大反应活性.这种同时把稳定性和反应活性有机地结合于一体的特质清楚地说明了锌指蛋白质分子对金属锌离子键合的专一性.
A density functional reactivity theory study has been carried out to elucidate the metalbinding specificity of zinc finger proteins. Three different zincfinger motif models, denoted by MS4-xNx（where M=divalent metal ions such as Mg, Ca, Sc, Ti, V, Cr, Mn, Fe, Co, Ni, Cu, and Zn, S represents the histidine residue, N stands for the cysteine residue, and x=0, 1, 2）. Results from all these model systems exhibit one unique feature of the zincfinger motif when the zinc divalent cation is bonded. That is, the Znbonded complex is both most stable and at the same time most reactive. This seamless combination of two often contradictory properties of a molecular system, stability and reactivity, explains the remarkable metalbinding specificity of the zincfinger proteins.
出处
《晓庄学院自然科学学报》
CAS
北大核心
2013年第2期44-48,共5页
Journal of Natural Science of Hunan Normal University
基金
晓庄学院"潇湘学者"杰出人才资助项目(23040609)
湖南省研究生创新项目(CX2012B223)
湖南省高校科技创新团队支持计划资助项目(湘教通[2012]318号)
关键词
锌指
密度泛函活性理论
金属键合专一性
zinc finger
density functional reactivity theory
metal-binding specificity
