The origin of protein interactions and allostery in colocalization

被引:303
作者
Kuriyan, John [1 ]
Eisenberg, David
机构
[1] Univ Calif Berkeley, Howard Hughes Med Inst, Calif Inst Quantitat Biosci, Dept Mol & Cell Biol, Berkeley, CA 94720 USA
[2] Univ Calif Berkeley, Howard Hughes Med Inst, Calif Inst Quantitat Biosci, Dept Chem, Berkeley, CA 94720 USA
[3] Lawrence Berkeley Lab, Phys Biosci Div, Berkeley, CA 94720 USA
[4] Univ Calif Los Angeles, Howard Hughes Med Inst, Los Angeles, CA 90095 USA
[5] Univ Calif Los Angeles, Dept Energy Inst Genom & Proteom, Inst Mol Biol, Dept Biol Chem, Los Angeles, CA 90095 USA
[6] Univ Calif Los Angeles, Dept Energy Inst Genom & Proteom, Inst Mol Biol, Dept Chem & Biochem, Los Angeles, CA 90095 USA
基金
美国国家科学基金会; 美国国家卫生研究院;
关键词
D O I
10.1038/nature06524
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
Two fundamental principles can account for how regulated networks of interacting proteins originated in cells. These are the law of mass action, which holds that the binding of one molecule to another increases with concentration, and the fact that the colocalization of molecules vastly increases their local concentrations. It follows that colocalization can amplify the effect on one protein of random mutations in another protein and can therefore, through natural selection, lead to interactions between proteins and to a startling variety of complex allosteric controls. It also follows that allostery is common and that homologous proteins can have different allosteric mechanisms. Thus, the regulated protein networks of organisms seem to be the inevitable consequence of natural selection operating under physical laws.
引用
收藏
页码:983 / 990
页数:8
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