FKBP公司
异构酶
脯氨酸异构酶
化学
肽基脯氨酰异构酶
脯氨酸
立体化学
背景(考古学)
酶
顺反异构体
突变体
生物化学
异构化
功能(生物学)
针脚1
生物
催化作用
氨基酸
细胞生物学
古生物学
基因
作者
Gunter Fischer,Thomas Tradler,Toralf Zarnt
出处
期刊:FEBS Letters
[Wiley]
日期:1998-04-10
卷期号:426 (1): 17-20
被引量:123
标识
DOI:10.1016/s0014-5793(98)00242-7
摘要
Polypeptides often display proline‐mediated conformational substates that are prone to isomer‐specific recognition and function. Both possibilities can be of biological significance. Distinct families of peptidyl prolyl cis/trans isomerases (PPIases) evolved proved to be highly specific for proline moieties arranged in a special context of subsites. Structural and chemical features of molecules specifically bound to the active site of PPIases served to improve catalysis of prolyl isomerization rather than ground state binding. For example, results inferred from receptor Ser/Thr or Tyr phosphorylation in the presence of site‐directed FKBP12 mutant proteins provided evidence for the crucial role of the enzymatic activity in down‐regulating function of FKBP12.
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