Molecular modeling studies of peptide inhibitors highlight the importance of conformational prearrangement for inhibition of calpain

Biochemistry

Volumn 49, Issue 26, 2010, Pages 5533-5539

  Jiao, Wanting ^a   McDonald, D Quentin ^a   Coxon, James M ^a   Parker, Emily J ^a  

^a UNIVERSITY OF CANTERBURY   (New Zealand)

Author keywords

[No Author keywords available]

Indexed keywords

ALZHEIMERS DISEASE; BRAIN TRAUMA; CALPAINS; CALPASTATIN; COMPUTATIONAL STUDIES; CONFORMATIONAL PREFERENCES; CYSTEINE PROTEASE; INHIBITORY ACTIVITY; INHIBITORY DOMAINS; LOOP REGIONS; MOLECULAR MODELING STUDIES; MUSCULAR DYSTROPHY; NATURALLY OCCURRING; OVER-EXPRESSION; PARKINSONS DISEASE; PEPTIDE INHIBITORS; SPINAL CORD INJURY; WILD TYPES;

CRYSTAL STRUCTURE;

PEPTIDES;

ALANINE; CALPAIN; CALPAIN 1; CALPASTATIN; CATHEPSIN L; GLUTAMIC ACID; LYSINE;

ARTICLE; CONFORMATION; CRYSTAL STRUCTURE; DRUG PROTEIN BINDING; ENZYME STRUCTURE; IC 50; MOLECULAR DYNAMICS; MONTE CARLO METHOD; PRIORITY JOURNAL; WILD TYPE;

CALCIUM-BINDING PROTEINS; CALPAIN; CRYSTALLOGRAPHY, X-RAY; CYSTEINE PROTEINASE INHIBITORS; HUMANS; MODELS, MOLECULAR; MUTATION; PEPTIDE FRAGMENTS; PEPTIDES; PROTEIN CONFORMATION;

EID: 77954185945     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi100048y     Document Type: Article

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