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Science 23 February 1996: Vol. 271. no. 5252, pp. 1081 - 1085 DOI: 10.1126/science.271.5252.1081
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Articles
The Galvanization of Biology: A Growing Appreciation for the
Roles of Zinc
Jeremy M. Berg
(1)
and
Yigong Shi
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.
The authors are in the Department of Biophysics and Biophysical
Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD
21205, USA.
(1) To whom correspondence should be addressed.
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Carcinogenesis
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