Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2052565 | FEBS Letters | 2005 | 4 Pages |
Abstract
SIB1 FKBP22 is a homodimer, with each subunit consisting of the C-terminal catalytic domain and N-terminal dimerization domain. This protein exhibits peptidyl prolyl cis–trans isomerase activity for both peptide and protein substrates. However, truncation of the N-terminal domain greatly reduces the activity only for a protein substrate. Using surface plasmon resonance, we showed that SIB1 FKBP22 loses the binding ability to a folding intermediate of protein upon truncation of the N-terminal domain but does not lose it upon truncation of the C-terminal domain. We propose that the binding site of SIB1 FKBP22 to a protein substrate of PPIase is located at the N-terminal domain.
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Authors
Yutaka Suzuki, Ohnmar Ye Win, Yuichi Koga, Kazufumi Takano, Shigenori Kanaya,