Solution conformation of a cyclophilin-bound proline isomerase substrate.
Solution conformation of a cyclophilin-bound proline isomerase substrate.
复制标题
亲环蛋白结合的脯氨酸异构酶底物的溶液构象。
DOI：
10.1021/bi00172a028
复制
发表时间：
1994
期刊：
影响因子：
2.9
通讯作者：
Armitage,IM
中科院分区：
文献类型：
--
作者：
Kakalis,LT;Armitage,IM
亲环素（CyP）是免疫抑制剂环孢菌素A（CsA）的17.8 kDa胞质受体，也是肽基脯氨酰顺反异构酶（PPI酶）。为了深入了解PPIase机制，通过二维1H NMR的转移核Overhauser效应（TRNOE）测量用于确定异构酶结合的标准模型底物suc-AAPF-pNA的构象。结果表明，与AP peptidebond的CyP结合的底物的m样构象不超过40平面。
Revised Manuscript Received November 8, 1993® abstract: Cyclophilin (CyP) is the 17.8-kDa cytosolic receptor of the immunosuppressant cyclosporin A (CsA) and also a peptidyl prolyl cis-trans isomerase (PPIase). In order to gain insights into the PPIase mechanism, transferred nuclear Overhauser effect (TRNOE) measurements by two-dimensional'H NMR were used to determine the conformation of the isomerase-bound standard model substrate suc-AAPF-pNA. Results indicate a m-like conformation for the CyP-bound substrate with the AP peptidebond being no more than 40 out of planarity.