The plasticity of the β-trefoil fold constitutes an evolutionary platform for protease inhibition

Journal of Biological Chemistry

Volumn 286, Issue 51, 2011, Pages 43726-43734

  Azarkan, Mohamed ^a   Martinez Rodriguez, Sergio ^b,c,d   Buts, Lieven ^b,c   Baeyens Volant, Danielle ^a   Garcia Pino, Abel ^b,c  

^a UNIVERSITÉ LIBRE DE BRUXELLES   (Belgium)

^b VRIJE UNIVERSITEIT BRUSSEL   (Belgium)

^c DEPARTMENT OF PLANT SYSTEMS BIOLOGY   (Belgium)

^d UNIVERSITY OF ALMERÍA   (Spain)

Author keywords

[No Author keywords available]

Indexed keywords

BIOPHYSICAL METHODS; CRUCIAL FUNCTIONS; PROTEASE ACTIVITIES; PROTEASE INHIBITION; PROTEASE INHIBITOR; SERINE PROTEASE; SPECIFIC INHIBITORS; STRUCTURAL BASIS; TRYPSIN INHIBITOR;

AMINO ACIDS;

ENZYME INHIBITION;

SERINE PROTEINASE; SERINE PROTEINASE INHIBITOR;

AMINO ACID SEQUENCE; ARTICLE; BETA TREFOIL FOLD; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME INHIBITION; ENZYME KINETICS; ENZYME STRUCTURE; MOLECULAR DOCKING; PLASTICITY; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN INTERACTION; SURFACE PLASMON RESONANCE; X RAY CRYSTALLOGRAPHY;

CARICA; CHYMOTRYPSIN; CRYSTALLOGRAPHY, X-RAY; ENZYME INHIBITORS; EVOLUTION, MOLECULAR; LATEX; PEPTIDE HYDROLASES; PROTEASE INHIBITORS; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN INTERACTION MAPPING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SCATTERING, RADIATION; SURFACE PLASMON RESONANCE; TRYPSIN;

EID: 83755171348     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.291310     Document Type: Article

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