The galvanization of biology: A growing appreciation for the roles of zinc

被引:1731
作者
Berg, JM
Shi, YG
机构
[1] Dept. Biophys. and Biophysical Chem., Johns Hopkins University, School of Medicine, Baltimore
关键词
D O I
10.1126/science.271.5252.1081
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
Zinc ions are key structural components of a large number of proteins. The binding of zinc stabilizes the folded conformations of domains so that they may facilitate interactions between the proteins and other macromolecules such as DNA. The modular nature of some of these zinc-containing proteins has allowed the rational design of site-specific DNA binding proteins. The ability of zinc to be bound specifically within a range of tetrahedral sites appears to be responsible for the evolution of the wide range of zinc-stabilized structural domains now known to exist. The lack of redox activity for the zinc ion and its binding and exchange kinetics also may be important in the use of zinc for specific functional roles.
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页码:1081 / 1085
页数:5
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