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FEBS Lett. 2005 Oct 24;579(25):5781-4. Epub 2005 Oct 6.

Binding analysis of a psychrotrophic FKBP22 to a folding intermediate of protein using surface plasmon resonance.

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  • 1Department of Material and Life Science, Graduate School of Engineering, Osaka University, Japan.


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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