Solution Conformation of a Cyclophilin-Bound Proline Isomerase Substrate

Lazaros T. Kakalis; Ian M. Armitage

doi:10.1021/bi00172a028

Solution Conformation of a Cyclophilin-Bound Proline Isomerase Substrate

Lazaros T. Kakalis, Ian M. Armitage

Biochemistry, Molecular Biology, and Biophysics (TMED)

Research output: Contribution to journal › Article › peer-review

15 Scopus citations

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° out of planarity.

Original language	English (US)
Pages (from-to)	1495-1501
Number of pages	7
Journal	Biochemistry
Volume	33
Issue number	6
DOIs	https://doi.org/10.1021/bi00172a028
State	Published - Feb 1 1994

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title = "Solution Conformation of a Cyclophilin-Bound Proline Isomerase Substrate",

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° out of planarity.",

author = "Kakalis, \{Lazaros T.\} and Armitage, \{Ian M.\}",

year = "1994",

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doi = "10.1021/bi00172a028",

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journal = "Biochemistry",

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T1 - Solution Conformation of a Cyclophilin-Bound Proline Isomerase Substrate

AU - Kakalis, Lazaros T.

AU - Armitage, Ian M.

PY - 1994/2/1

Y1 - 1994/2/1

N2 - 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° out of planarity.

AB - 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° out of planarity.

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VL - 33

SP - 1495

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JO - Biochemistry

JF - Biochemistry

IS - 6

ER -

Solution Conformation of a Cyclophilin-Bound Proline Isomerase Substrate

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