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C almodulin EF‐hand peptides as Ca 2+ ‐switchable recognition tags
Author(s) -
Oku Akihiko,
Imanishi Miki,
Noshiro Daisuke,
Murayama Tomo,
Takeuchi Toshihide,
Nakase Ikuhiko,
Futaki Shiroh
Publication year - 2017
Publication title -
peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.22937
Subject(s) - chemistry , ef hand , calmodulin , peptide , biophysics , disulfide bond , calcium binding protein , target peptide , crystallography , stereochemistry , biochemistry , calcium , enzyme , organic chemistry , biology
Calmodulin is a representative calcium‐binding protein comprised of four Ca 2+ ‐binding motifs with a helix‐loop‐helix structure (EF‐hands). In this study, we clarified the potential of peptide segments derived from the third and fourth EF‐hands (EF3 and EF4) to act as recognition tags. Through an analysis of the mode of disulfide formation among cysteines inserted at the N‐ or C‐terminus of these peptide segments, EF3 and EF4 peptides were suggested to form a heterodimer with a topology similar to that in the wild‐type protein. Heterodimer formation was shown to be a function of the Ca 2+ concentration, suggesting that these structures may be used as Ca 2+ ‐switchable recognition tags. An example of an “EF‐tag” system involving the membrane fusion of liposomes decorated with EF3 and EF4 peptides is presented. © 2016 Wiley Periodicals, Inc. Biopolymers (Pept Sci), 2016.