How does heparin prevent the pH inactivation of cathepsin B? Allosteric mechanism elucidated by docking and molecular dynamics

BMC Genomics

Volumn 11, Issue SUPPL. 5, 2010, Pages

  Costa, Mauricio G S ^a   Batista, Paulo R ^a   Shida, Cláudio S ^a,b   Robert, Charles H ^c   Bisch, Paulo M ^a   Pascutti, Pedro G ^a  

^a FEDERAL UNIVERSITY OF RIO DE JANEIRO   (Brazil)

^b UNIVERSIDADE DE MOGI DAS CRUZES   (Brazil)

^c INST DE BIOLOGIE PHYSICO CHIMIQUE   (France)

Author keywords

[No Author keywords available]

Indexed keywords

CATHEPSIN B; HEPARIN;

ACIDITY; ALKALINITY; ALLOSTERISM; ARTICLE; BINDING SITE; CATALYSIS; ENZYME ACTIVE SITE; ENZYME INACTIVATION; ENZYME REGULATION; ENZYME STABILITY; ENZYME STRUCTURE; HYDROGEN BOND; IONIZATION; MOLECULAR DOCKING; MOLECULAR DYNAMICS; PH; PROTEIN DOMAIN; PROTEIN LOCALIZATION; PROTEIN STABILITY; PROTON TRANSPORT; STATIC ELECTRICITY; CHEMICAL STRUCTURE; CHEMISTRY; GENETICS; METABOLISM; PHYSIOLOGY;

ALLOSTERIC REGULATION; BINDING SITES; CATHEPSIN B; ENZYME STABILITY; HEPARIN; HYDROGEN-ION CONCENTRATION; MODELS, MOLECULAR; MOLECULAR DYNAMICS SIMULATION; STATIC ELECTRICITY;

EID: 78650818858     PISSN: None     EISSN: 14712164     Source Type: Journal    
DOI: 10.1186/1471-2164-11-S5-S5     Document Type: Article

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