The -Cys-X1-X2-Cys- motif of reduced glutaredoxins adopts a consensus structure that explains the low p K a of its catalytic cysteine

Biochemistry

Volumn 51, Issue 41, 2012, Pages 8189-8207

  Foloppe, Nicolas ^a   Vlamis Gardikas, Alexios ^b   Nilsson, Lennart ^c  

^a University of Patras ^*  (United Kingdom)

^b UNIVERSITY OF PATRAS   (Greece)

^c KAROLINSKA INSTITUTE   (Sweden)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CONFORMATIONS; ESCHERICHIA COLI; HYDROGEN BONDS; MOLECULAR DYNAMICS; NUCLEAR MAGNETIC RESONANCE; VIRUSES;

CATALYTIC CYSTEINES; CONFORMATIONAL DYNAMICS; EXPERIMENTAL INVESTIGATIONS; MOLECULAR-DYNAMICS MODEL; NMR STRUCTURES; NUCLEAR MAGNETIC RESONANCE(NMR); STRUCTURAL MODELS; SUBSTRATE RECOGNITION;

ENZYMES;

CYSTEINE; GLUTAREDOXIN; GLUTAREDOXIN 1; GLUTAREDOXIN 2; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ARTICLE; CATALYSIS; CATALYST; CONTROLLED STUDY; ENZYME POLYMORPHISM; ENZYME PURIFICATION; ESCHERICHIA COLI; HYDROGEN BOND; MOLECULAR DYNAMICS; MOLECULAR STABILITY; MUTANT; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN MOTIF; PROTEIN STRUCTURE;

EID: 84867507044     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi3006576     Document Type: Article

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