High-resolution insights into binding of unfolded polypeptides by the PPIase chaperone SlpA
SlpA is a 2-domain protein consisting of an FK506-binding protein (FKBP) domain that harbors the peptidyl-prolyl cis/trans-isomerase (PPIase) active site and a small insert-in-flap (IF) domain that endows the protein with chaperone activity. We have determined the structure of SlpA from Escherichia...
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Main Authors: | Löw, Christian, Nordlund, Pär, Quistgaard, Esben M. |
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Other Authors: | School of Biological Sciences |
Format: | Article |
Language: | English |
Published: |
2013
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Subjects: | |
Online Access: | https://hdl.handle.net/10356/100451 http://hdl.handle.net/10220/16249 |
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Institution: | Nanyang Technological University |
Language: | English |
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