Crystal structure of mammalian selenocysteine-dependent iodothyronine deiodinase suggests a peroxiredoxin-like catalytic mechanism

Proceedings of the National Academy of Sciences of the United States of America

Volumn 111, Issue 29, 2014, Pages 10526-10531

  Schweizer, Ulrich ^a   Schlicker, Christine ^b   Braun, Doreen ^a   Köhrle, Josef ^c   Steegborn, Clemens ^d  

^a UNIVERSITY OF BONN   (Germany)

^b RUHR UNIVERSITY BOCHUM   (Germany)

^c CHARITÉ UNIVERSITÄTSMEDIZIN BERLIN   (Germany)

^d UNIVERSITY OF BAYREUTH   (Germany)

Author keywords

Iodothyronine deiodination; Selenenyl sulfide; Selenoprotein; Thiol cofactor; Thioredoxin fold

Indexed keywords

DEIODINASE 3; IODOTHYRONINE; IODOTHYRONINE DEIODINASE; OXIDOREDUCTASE; PEROXIREDOXIN; SELENOCYSTEINE; THIOREDOXIN; UNCLASSIFIED DRUG;

ALKYLATION; ARTICLE; BINDING SITE; CATALYSIS; CRYSTAL STRUCTURE; DEIODINATION; DIMERIZATION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME SUBSTRATE COMPLEX; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DEGRADATION; PROTEIN SECONDARY STRUCTURE; PROTON TRANSPORT;

IODOTHYRONINE DEIODINATION; SELENENYL-SULFIDE; SELENOPROTEIN; THIOL COFACTOR; THIOREDOXIN FOLD;

ANIMALS; BIOCATALYSIS; CRYSTALLOGRAPHY, X-RAY; HYDROGEN BONDING; IODIDE PEROXIDASE; ISOMERISM; MICE; OXIDATION-REDUCTION; PEROXIREDOXINS; PROTEIN MULTIMERIZATION; PROTONS; SELENOCYSTEINE;

EID: 84904595367     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1323873111     Document Type: Article

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