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- W2046875506 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." @default.
- W2046875506 created "2016-06-24" @default.
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- W2046875506 date "2005-10-06" @default.
- W2046875506 modified "2023-10-13" @default.
- W2046875506 title "Binding analysis of a psychrotrophic FKBP22 to a folding intermediate of protein using surface plasmon resonance" @default.
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- W2046875506 doi "https://doi.org/10.1016/j.febslet.2005.09.067" @default.
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