STABILIZATION OF THE FK506 BINDING-PROTEIN BY LIGAND-BINDING

被引：13

作者：

MARQUISOMER, D

SANYAL, G

VOLKIN, DB

MARCY, AI

CHAN, HK

RYAN, JA

MIDDAUGH, CR

机构：

[1] MERCK SHARP & DOHME LTD,DEPT BIOPHYS CHEM,W POINT,PA 19486

[2] MERCK SHARP & DOHME LTD,DEPT PHARMACEUT RES,RAHWAY,NJ 07065

[3] MERCK SHARP & DOHME LTD,DEPT BIOPHYS CHEM,RAHWAY,NJ 07065

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1991年 / 179卷 / 02期

关键词：

D O I：

10.1016/0006-291X(91)91879-H

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：

Although the rotamase activity of the FK506 binding protein is inhibited by ligand binding, it is hypothesized that the ligand/protein complex itself may be responsible for the immunosuppressive effects of FK506. We have therefore examined the structure of the FK506 binding protein in the presence of an analog of FK506 (FK520) by a combination of fluorescence, CD, FTIR and calorimetry. While only small changes in the overall structure of the protein may be induced by ligand, a large change in thermal stability of the binding protein is observed. © 1991.

引用

页码：741 / 748

页数：8

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