Binding analysis of a psychrotrophic FKBP22 to a folding intermediate of protein using surface plasmon resonance |
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Authors: | Suzuki Yutaka Win Ohnmar Ye Koga Yuichi Takano Kazufumi Kanaya Shigenori |
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Affiliation: | Department of Material and Life Science, Graduate School of Engineering, Osaka University, Japan. |
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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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Keywords: | PPIase, peptidyl prolyl cis-trans isomerase FKBP, FK506-binding protein RU, resonance unit DTT, dithiothreitol |
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