Functions of the Hsp90-Binding FKBP Immunophilins
Sub-cellular biochemistry(2015)
摘要
Hsp90 functionally interacts with a broad array of client proteins, but in every case examined Hsp90 isaccompanied by one or
more co-chaperones. One class of co-chaperone contains a tetratricopeptide repeat domain that targets the co-chaperone to
the C-terminal region of Hsp90. Within this class are Hsp90-binding peptidylprolyl isomerases, most of which belong to the
FK506-binding protein (FKBP) family. Despite the common association of FKBP co-chaperones with Hsp90, it is now clear that
the client protein influences, and is influenced by, the particular FKBP bound to Hsp90. Examples include Xap2 in aryl hydrocarbon
receptor complexes and FKBP52 in steroid receptor complexes. In this chapter, we discuss the known functional roles played
by FKBP co-chaperones and, where possible, relate distinctive functions to structural differences between FKBP members.
更多查看译文
AI 理解论文
溯源树
样例
![](https://originalfileserver.aminer.cn/sys/aminer/pubs/mrt_preview.jpeg)
生成溯源树,研究论文发展脉络
Chat Paper
正在生成论文摘要