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.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Isomerases / chemistry*
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Amino Acid Isomerases / metabolism
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Amino Acid Sequence
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Binding Sites
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Carrier Proteins / chemistry*
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Carrier Proteins / metabolism
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Deuterium
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Magnetic Resonance Spectroscopy*
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Molecular Sequence Data
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Molecular Structure
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Oligopeptides / chemistry*
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Oligopeptides / metabolism
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Peptidylprolyl Isomerase
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Protein Conformation
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Recombinant Proteins / metabolism
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Solutions*
Substances
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Carrier Proteins
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Oligopeptides
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Recombinant Proteins
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Solutions
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succinyl-alanyl-alanyl-prolyl-phenylalanine-4-nitroanilide
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Deuterium
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Amino Acid Isomerases
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Peptidylprolyl Isomerase