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Solution conformation of a cyclophilin-bound proline isomerase substrate.

作者信息

Kakalis L T, Armitage I M

机构信息

Department of Pharmacology, Yale University Medical School, New Haven, Connecticut 06520-8066.

出版信息

Biochemistry. 1994 Feb 15;33(6):1495-501. doi: 10.1021/bi00172a028.

DOI:10.1021/bi00172a028
PMID:8312269
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 1H NMR were used to determine the conformation of the isomerase-bound standard model substrate suc-AAPF-pNA. Results indicate a cis-like conformation for the CyP-bound substrate with the A-P peptide bond being no more than 40 degrees out of planarity.

摘要

相似文献

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Solution conformation of a cyclophilin-bound proline isomerase substrate.
Biochemistry. 1994 Feb 15;33(6):1495-501. doi: 10.1021/bi00172a028.
2
Peptidyl-prolyl cis-trans isomerase activity as studied by dynamic proton NMR spectroscopy.通过动态质子核磁共振光谱研究肽基脯氨酰顺反异构酶活性。
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1H, 13C and 15N backbone assignments of cyclophilin when bound to cyclosporin A (CsA) and preliminary structural characterization of the CsA binding site.与环孢菌素A（CsA）结合时亲环蛋白的1H、13C和15N主链归属以及CsA结合位点的初步结构表征。
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Isotope-edited NMR of cyclosporin A bound to cyclophilin: evidence for a trans 9,10 amide bond.与亲环蛋白结合的环孢菌素A的同位素编辑核磁共振：反式9,10酰胺键的证据。
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Structure of human cyclophilin and its binding site for cyclosporin A determined by X-ray crystallography and NMR spectroscopy.通过X射线晶体学和核磁共振光谱法确定的人亲环蛋白的结构及其与环孢菌素A的结合位点。
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Biochemistry. 1996 Mar 19;35(11):3636-40. doi: 10.1021/bi9520803.

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