The substrate-binding site in Escherichia coli cyclophilin A preferably recognizes a cis-proline isomer or a highly distorted form of the trans isomer

Journal of Molecular Biology

Volumn 256, Issue 5, 1996, Pages 897-908

  Konno, Michiko ^a   Ito, Mariko ^a   Hayano, Toshiya ^b   Takahashi, Nobuhiro ^b  

^a OCHANOMIZU UNIVERSITY   (Japan)

^b Development Laboratory Tonen K K   (Japan)

Author keywords

Cyclophilin A; Cyclosporin A; FK506 binding protein; Peptidyl prolyl cis trans isomerase; Protein crystal structure

Indexed keywords

BACTERIAL ENZYME; CYCLOPHILIN A; CYCLOSPORIN A; TRIPEPTIDE;

AMINO ACID SEQUENCE; ARTICLE; BINDING AFFINITY; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME BINDING; ENZYME CONFORMATION; ENZYME SUBSTRATE COMPLEX; ESCHERICHIA COLI; HYDROPHOBICITY; MOLECULAR RECOGNITION; NONHUMAN; PRIORITY JOURNAL; STEREOSPECIFICITY; STRUCTURE ACTIVITY RELATION;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 0029970349     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1996.0136     Document Type: Article

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