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Protein Engineering vol. 16 no. 6 pp. 429-434, 2003
© 2003 Oxford University Press

A grafting approach to obtain site-specific metal-binding properties of EF-hand proteins

Yiming Ye1, Sarah Shealy1, Hsiau-Wei Lee1, Ivan Torshin2, Robert Harrison3 and Jenny J. Yang1,4

1Department of Chemistry, Center of Drug Design, 2Department of Biology and 3Department of Computer Science, Georgia State University, Atlanta, GA 30303, USA

4 To whom correspondence should be addressed. e-mail: chejjy{at}panther.gsu.edu

The EF-hand calcium-binding loop III from calmodulin was inserted with glycine linkers into the scaffold protein CD2.D1 at three locations to study site-specific calcium binding properties of EF-hand motifs. After insertion, the host protein retains its native structure and forms a 1:1 metal–protein complex for calcium and its analog, lanthanum. Tyrosine-sensitized Tb3+ energy transfer exhibits metal binding and La3+ and Ca2+ compete for the metal binding site. The grafted EF-loop III in different environments has similar La3+ binding affinities, suggesting that it is largely solvated and functions independently from the host protein.

Received May 25, 2002; revised January 23, 2003; accepted April 25, 2003.


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