Insights into Immunophilin Structure and Function

被引：18

作者：

Luecke, C. ^{[1
]}

Weiwad, M. ^{[1
]}

机构：

[1] Max Planck Res Unit Enzymol Prot Folding, D-06120 Halle, Saale, Germany

来源：

CURRENT MEDICINAL CHEMISTRY | 2011年 / 18卷 / 35期

关键词：

Calcineurin; cyclophilin; FK506-binding protein; immunophilin; immunosuppression; PPIase domain; HEPATITIS-C-VIRUS; X-RAY-STRUCTURE; CALCIUM-RELEASE CHANNEL; FK506; BINDING-PROTEIN; CIS-TRANS ISOMERASE; MITOCHONDRIAL PERMEABILITY TRANSITION; PEPTIDYL-PROLYL ISOMERASE; NMR SOLUTION STRUCTURE; HUMAN CYCLOPHILIN-A; MACROPHAGE INFECTIVITY POTENTIATOR;

D O I：

10.2174/092986711798194324

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The immunophilins are proteins which are capable of influencing the immune response in combination with an immunosuppressive drug. Their natural function, however, is mainly the cis/trans isomerization of peptidyl-prolyl bonds in other proteins. This review lists all immunophilin structure coordinates currently available in the RCSB protein data bank and highlights the key active-site factors that define their catalytic and immunological action. In addition, an overview of biologically-relevant functions is provided for various immunophilin members.

引用

页码：5333 / 5354

页数：22

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