Crystal structures of barley thioredoxin h isoforms HvTrxh1 and HvTrxh2 reveal features involved in protein recognition and possibly in discriminating the isoform specificity

Protein Science

Volumn 17, Issue 6, 2008, Pages 1015-1024

  Maeda, Kenji ^a   Hägglund, Per ^a   Finnie, Christine ^a   Svensson, Birte ^a   Henriksen, Anette ^b  

^a TECHNICAL UNIVERSITY OF DENMARK   (Denmark)

^b CARLSBERG LABORATORY   (Denmark)

Author keywords

Cysteine oxidoreduction; Protein recognition; Redox regulation; Thioredoxin h

Indexed keywords

ARGININE; CYSTEINE; DISULFIDE; GLUTAMIC ACID; HYDROGEN; ISOLEUCINE; ISOPROTEIN; METHIONINE; SULFUR; THIOL; THIOREDOXIN; THIOREDOXIN H;

ARTICLE; ATOM; BARLEY; BETA SHEET; CRYSTAL STRUCTURE; HYDROGEN BOND; HYDROPHOBICITY; MOLECULAR RECOGNITION; NUCLEOTIDE SEQUENCE; OXIDATION; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN ENGINEERING; PROTEIN FOLDING; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; RADIATION; SEQUENCE HOMOLOGY;

AMINO ACID SEQUENCE; CATALYSIS; CRYSTALLOGRAPHY, X-RAY; DIMERIZATION; ELECTROSTATICS; HORDEUM; ISOENZYMES; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; OXIDATION-REDUCTION; PROTEIN CONFORMATION; SEQUENCE HOMOLOGY, AMINO ACID; SUBSTRATE SPECIFICITY; THIOREDOXIN H;

EMBRYOPHYTA; HORDEUM;

EID: 44349183189     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1110/ps.083460308     Document Type: Article

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