Femtomolar Zn(II) affinity of minimal zinc hook peptides--a promising small tag for protein engineering

Chem Commun (Camb). 2013 Feb 14;49(13):1312-4. doi: 10.1039/c2cc38174e. Epub 2013 Jan 10.

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

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Motifs
  • Amino Acid Sequence
  • Archaeal Proteins / chemistry
  • Archaeal Proteins / genetics
  • DNA-Binding Proteins / chemistry
  • DNA-Binding Proteins / genetics
  • Peptide Fragments / chemistry
  • Peptide Fragments / metabolism*
  • Protein Engineering / methods*
  • Protein Multimerization
  • Protein Structure, Quaternary
  • Pyrococcus furiosus
  • Zinc / metabolism*

Substances

  • Archaeal Proteins
  • DNA-Binding Proteins
  • Peptide Fragments
  • Zinc