Molecular insight into the role of the leucine residue on the L2 loop in the catalytic activity of caspases 3 and 7

Bioscience Reports

Volumn 32, Issue 3, 2012, Pages 305-313

  Kang, Hyo Jin ^a,b   Lee, Young Mi ^b   Jeong, Myeong Seon ^a,b   Kim, Moonil ^b   Bae, Kwang Hee ^b   Kim, Seung Jun ^b   Chung, Sang J ^a,b  

^a University of Science and Technology (UST)   (South Korea)

^b Korea Research Institute of Bioscience and Biotechnology (KRIBB)   (South Korea)

Author keywords

Apoptosis; Caspase; Crystal structure; Hydrophobic interaction; Proenzyme activation; Tryptophan fluorescence

Indexed keywords

ALANINE; ASPARTIC ACID; CASPASE 3; CASPASE 7; LEUCINE; PHENYLALANINE; TRYPTOPHAN; TYROSINE; VALINE;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; APOPTOSIS; ARTICLE; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVATION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME CONFORMATION; ENZYME INACTIVATION; ENZYME MECHANISM; ENZYME SPECIFICITY; ENZYME STABILITY; FLUORESCENCE SPECTROSCOPY; HYDROPHOBICITY; MOLECULAR DYNAMICS; PROTEIN EXPRESSION; RESIDUE ANALYSIS; SIGNAL TRANSDUCTION; SITE DIRECTED MUTAGENESIS; STRUCTURAL HOMOLOGY; WILD TYPE; X RAY CRYSTALLOGRAPHY;

AMINO ACID MOTIFS; AMINO ACID SUBSTITUTION; CASPASE 3; CASPASE 7; CATALYTIC DOMAIN; CLONING, MOLECULAR; CRYSTALLOGRAPHY, X-RAY; HYDROGEN BONDING; KINETICS; LEUCINE; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; PROTEIN PRECURSORS; SPECTROMETRY, FLUORESCENCE; TRYPTOPHAN;

EID: 84859450398     PISSN: 01448463     EISSN: 15734935     Source Type: Journal    
DOI: 10.1042/BSR20120009     Document Type: Article

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