Structural and mechanistic insights into a novel non-competitive Kunitz trypsin inhibitor from Adenanthera pavonina L. seeds with double activity toward serine- and cysteine-proteinases

Journal of Molecular Graphics and Modelling

Volumn 29, Issue 2, 2010, Pages 148-156

  Migliolo, Ludovico ^a,b   de Oliveira, Adeliana S ^a   Santos, Elizeu A ^a   Franco, Octavio L ^b,c   de Sales, Maurício P ^a  

^a FEDERAL UNIVERSITY OF RIO GRANDE DO NORTE   (Brazil)

^b UNIVERSIDADE CATÓLICA DE BRASÍLIA   (Brazil)

^c FEDERAL UNIVERSITY OF JUIZ DE FORA   (Brazil)

Author keywords

Adenanthera pavonina; Binding sites; Docking studies; Homology modeling; Kunitz family; Non competitive proteinase inhibitor

Indexed keywords

ACTION MECHANISMS; ADENANTHERA PAVONINA; ADJACENT SITES; BIFUNCTIONAL INHIBITORS; COMPETITIVE ACTIVITY; HIGH RESOLUTION; HOMOLOGY MODELING; IN-SILICO; IN-VITRO ASSAYS; INHIBITORY ACTIVITY; INTERACTION MODES; INTERACTION SITE; KUNITZ FAMILY; KUNITZ TRYPSIN INHIBITORS; MOLECULAR EXCLUSION; PROTEINASE INHIBITORS; TERNARY COMPLEX; THREE-DIMENSIONAL STRUCTURE;

AGRICULTURAL PRODUCTS; AMINO ACIDS; BINDING ENERGY; BIOCHEMISTRY; CATALYSTS; DOCKING; ENZYME INHIBITION; ENZYMES; PHOSPHATASES; PURIFICATION; SIZE EXCLUSION CHROMATOGRAPHY; THREE DIMENSIONAL;

BINDING SITES;

ADENANTHERA PAVONINA EXTRACT; ARGININE; CYSTEINE PROTEINASE; CYSTEINE PROTEINASE INHIBITOR; LYSINE; PAPAIN; PLANT EXTRACT; SERINE; SERINE PROTEINASE; SERINE PROTEINASE INHIBITOR; TRYPSIN; UNCLASSIFIED DRUG;

ADENANTHERA PAVONINA; ARTICLE; BINDING SITE; CHROMATOGRAPHY; DOSE RESPONSE; DRUG BINDING SITE; DRUG PROTEIN BINDING; DRUG SPECIFICITY; DRUG STRUCTURE; DRUG TARGETING; ENZYME INHIBITION; HUMAN; IN VITRO STUDY; LEGUME; MOLECULAR DOCKING; MOLECULAR INTERACTION; MOLECULAR MODEL; MOLECULAR WEIGHT; NONHUMAN; PLANT SEED; PRIORITY JOURNAL;

AMINO ACID SEQUENCE; CYSTEINE PROTEASES; FABACEAE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PAPAIN; PEPTIDES; PLANT PROTEINS; SEEDS; SEQUENCE ALIGNMENT; SERINE PROTEASES; TITRIMETRY; TRYPSIN;

ADENANTHERA PAVONINA;

EID: 77956285190     PISSN: 10933263     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmgm.2010.05.006     Document Type: Article

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