Requirements for peptidyl-prolyl isomerization activity: A comprehensive mutational analysis of the substrate-binding cavity of FK506-binding protein 12

Protein Science

Volumn 16, Issue 12, 2007, Pages 2618-2625

  Ikura, Teikichi ^a   Ito, Nobutoshi ^a  

^a TOKYO MEDICAL AND DENTAL UNIVERSITY   (Japan)

Author keywords

Comprehensive mutational analysis; Human FK506 binding protein 12; Peptidyl prolyl isomerase; Substrate binding cavity

Indexed keywords

AMINO ACID; ARGININE; ASPARAGINE; CHYMOTRYPSIN; FK 506 BINDING PROTEIN; FK 506 BINDING PROTEIN 12; MUTANT PROTEIN; PEPTIDE; PEPTIDYLPROLYL ISOMERASE; PHENYLALANINE; TRYPTOPHAN; UNCLASSIFIED DRUG; VALINE;

AMINO ACID SUBSTITUTION; ARTICLE; BINDING SITE; COMPLEX FORMATION; CRYSTAL STRUCTURE; ENZYME ACTIVITY; ENZYME SUBSTRATE; HYDROPHOBICITY; ISOMERIZATION; MUTATIONAL ANALYSIS; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DETERMINATION; WILD TYPE;

AMINO ACID SUBSTITUTION; BINDING SITES; HUMANS; MODELS, MOLECULAR; MUTATION; PEPTIDES; PROTEIN CONFORMATION; SUBSTRATE SPECIFICITY; TACROLIMUS BINDING PROTEIN 1A;

EID: 36448957938     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1110/ps.073203707     Document Type: Article

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