An intersubunit lock-and-key 'Clasp' motif in the dimer interface of Delta class glutathione transferase

Biochemical Journal

Volumn 394, Issue 1, 2006, Pages 135-144

  Wongsantichon, Jantana ^a   Ketterman, Albert J ^a  

^a MAHIDOL UNIVERSITY   (Thailand)

Author keywords

Anopheles dirus; Aromatic ring stacking; Glutathione transferase; Lock and key; Pi pi interaction; Subunit interface

Indexed keywords

AROMATIC COMPOUNDS; CATALYSIS; CONFORMATIONS; DIMERIZATION; HYDROPHOBICITY;

ANOPHELES DIRUS; AROMATIC RING STACKING; GLUTATHIONE TRANSFERASE; LOCK-AND-KEY; PI-PI INTERACTION; SUBUNIT INTERFACE;

ENZYMES;

GLUTATHIONE; GLUTATHIONE TRANSFERASE; PROTEIN SUBUNIT;

AMINO ACID SUBSTITUTION; ANOPHELES; ARTICLE; CONFORMATIONAL TRANSITION; ENZYME ACTIVE SITE; ENZYME ANALYSIS; ENZYME CONFORMATION; ENZYME KINETICS; ENZYME STRUCTURE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN INTERACTION; PROTEIN MOTIF; PROTEIN QUATERNARY STRUCTURE;

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; ANIMALS; ANOPHELES; BINDING SITES; GENE EXPRESSION REGULATION, ENZYMOLOGIC; GLUTATHIONE TRANSFERASE; KINETICS; MODELS, MOLECULAR; PROTEIN BINDING; PROTEIN ENGINEERING; SEQUENCE HOMOLOGY, AMINO ACID; SUBSTRATE SPECIFICITY;

ANOPHELES DIRUS; INSECTA; MAMMALIA;

EID: 32944456314     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20050915     Document Type: Article

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