Abstract
The minimal zinc hook peptide of Rad50 and its alanine mutants form highly stable Zn(II) complexes. These peptides were successfully used as a small, efficient tag for reversible Zn(II)-mediated protein homodimerization. The high stability, its biological consequences and potential applications in protein engineering are discussed.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Motifs
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Amino Acid Sequence
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Archaeal Proteins / chemistry
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Archaeal Proteins / genetics
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DNA-Binding Proteins / chemistry
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DNA-Binding Proteins / genetics
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Peptide Fragments / chemistry
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Peptide Fragments / metabolism*
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Protein Engineering / methods*
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Protein Multimerization
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Protein Structure, Quaternary
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Pyrococcus furiosus
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Zinc / metabolism*
Substances
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Archaeal Proteins
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DNA-Binding Proteins
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Peptide Fragments
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Zinc