Title : Secondary structure and backbone resonance assignments of the periplasmic cyclophilin type peptidyl-prolyl isomerase from Escherichia coli.

Pub. Date : 1993 Jun 29

PMID : 8518284






1 Functional Relationships(s)
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Protein Name
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1 Sequence alignment with human T-cell cyclophilin based on secondary structure homology implicates several residues in E. coli cyclophilin that may be crucial for binding the peptide substrate AC-A-A-P-A-AMC and the immunosuppressive drug cyclosporin A. Cyclosporine peptidylprolyl isomerase A Homo sapiens