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The X‐ray structure of a tetrapeptide bound to the active site of human cyclophilin A
Author(s) -
Kallen Joerg,
Walkinshaw Malcolm D.
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)80865-e
Subject(s) - tetrapeptide , dimer , cyclophilin , isomerase , chemistry , stereochemistry , cyclophilin a , active site , crystallography , peptidylprolyl isomerase , substrate (aquarium) , prolyl isomerase , molecule , enzyme , biochemistry , pin1 , biology , microbiology and biotechnology , peptide , organic chemistry , ecology , gene
Human cyclophilin A (165 residues) has peptidyl‐prolyl cis‐trans isomerase activity. Here we report a high‐resolution three‐dimensional X‐ray structure of a substrate, ac‐Ala‐Ala‐Pro‐Ala‐amc (ac. acetyl: amc. amidomethylcoumarin) bound to the active‐site of cyclophilin. The structure consisting of a dimer of complexes and 135 water molecules was refined to a crystallographic R‐factor of 17.7% for all data in the range 8 Å‐2.3 Å.