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  • Title: Binding analysis of a psychrotrophic FKBP22 to a folding intermediate of protein using surface plasmon resonance.
    Author: Suzuki Y, Win OY, Koga Y, Takano K, Kanaya S.
    Journal: FEBS Lett; 2005 Oct 24; 579(25):5781-4. PubMed ID: 16223489.
    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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