Crystal structure of human thioredoxin revealing an unraveled helix and exposed S-nitrosation site

Protein Science

Volumn 19, Issue 9, 2010, Pages 1801-1806

  Weichsel, Andrzej ^a   Kem, Michelle ^a   Montfort, William R ^a  

^a University of Arizona   (United States)

Author keywords

Nitrosylation; Oxidation; Protein dynamics; Reduction; Signaling pathways; Unfolding

Indexed keywords

CYSTEINE; DISULFIDE; HYDROGEN; MUTANT PROTEIN; SERINE; THIOREDOXIN;

ANIMAL CELL; ARTICLE; BINDING SITE; CONTROLLED STUDY; CRYSTAL STRUCTURE; DISULFIDE BOND; HYDROGEN BOND; MOLECULE; NITROSATION; NONHUMAN; OXIDATION REDUCTION REACTION; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN LOCALIZATION; PROTEIN STABILITY; PROTEIN STRUCTURE; TRIPLE HELIX;

CRYSTALLOGRAPHY, X-RAY; HUMANS; MODELS, MOLECULAR; MUTATION; NITROSATION; OXIDATION-REDUCTION; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN UNFOLDING; THIOREDOXINS;

EID: 77956366486     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.455     Document Type: Article

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