Molecular insights into substrate recognition and catalytic mechanism of the chaperone and FKBP peptidyl-prolyl isomerase SlyD

Molecular insights into substrate recognition and catalytic mechanism of the chaperone and FKBP peptidyl-prolyl isomerase SlyD

Background: Peptidyl-prolyl isomerases (PPIases) catalyze cis/trans isomerization of peptidyl-prolyl bonds, which is often rate-limiting for protein folding. SlyD is a two-domain enzyme containing both a PPIase FK506-binding protein (FKBP) domain and an insert-in-flap (IF) chaperone domain. To date,...

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書目詳細資料
Main Authors:	Quistgaard, Esben M., Weininger, Ulrich, Ural-Blimke, Yonca, Modig, Kristofer, Nordlund, Pär, Akke, Mikael, Löw, Christian
其他作者:	School of Biological Sciences
格式:	Article
語言:	English
出版:	2016
主題:	Peptidyl-prolyl isomerase (PPIase) FK506-binding protein (FKBP)
在線閱讀:	https://hdl.handle.net/10356/84105 http://hdl.handle.net/10220/41603
標簽:	添加標簽沒有標簽, 成為第一個標記此記錄!
機構:	Nanyang Technological University
語言:	English

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