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First Crystal Structure of a Medicinally Relevant Gold Protein Complex: Unexpected Binding of [Au(PEt 3 )] + to Histidine
Author(s) -
Zou Juan,
Taylor Paul,
Dornan Jacqueline,
Robinson Stephen P.,
Walkinshaw Malcolm D.,
Sadler Peter J.
Publication year - 2000
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/1521-3773(20000818)39:16<2931::aid-anie2931>3.0.co;2-w
Subject(s) - histidine , enzyme , residue (chemistry) , stereochemistry , chemistry , adduct , isomerase , cyclophilin , thiol , active site , biochemistry , binding site , organic chemistry , gene
Unexpectedly, not interested in sulfur : the antiarthritic complex [Au(PEt 3 )Cl] ( 1 ) reacts with crystals of cyclophilin‐3 (Cyp‐3), a peptidyl prolyl isomerase enzyme linked to cellular stress responses, to form an N ε ‐bound [AuPEt 3 ] + adduct with the active site residue His 133, despite the presence of four Cys thiol groups in the protein. Complex 1 is a potent inhibitor of the enzyme (IC 50 =14 n M ).