Inactivating mutation in histone deacetylase 3 stabilizes its active conformation

Protein Science

Volumn 22, Issue 10, 2013, Pages 1306-1312

  Arrar, Mehrnoosh ^a   De Oliveira, Cesar Augusto F ^a   McCammon, J Andrew ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

Allostery; Conformational selection; HDAC3; Molecular recognition; R265P

Indexed keywords

DEACETYLASE ACTIVATING DOMAIN PROTEIN; HISTONE DEACETYLASE 3; INOSITOL TETRAKISPHOSPHATE; PROTEIN; UNCLASSIFIED DRUG;

ARTICLE; CONFORMATIONAL TRANSITION; ENZYME ACTIVATION; ENZYME ACTIVITY; ENZYME CONFORMATION; ENZYME SPECIFICITY; ENZYME STABILITY; GENE MUTATION; PRIORITY JOURNAL; PROTEIN BINDING;

ALLOSTERY; CONFORMATIONAL SELECTION; HDAC3; MOLECULAR RECOGNITION; R265P;

AMINO ACID SUBSTITUTION; ARGININE; CATALYTIC DOMAIN; ENZYME ACTIVATION; ENZYME STABILITY; HISTONE DEACETYLASES; HUMANS; INOSITOL PHOSPHATES; MODELS, MOLECULAR; MOLECULAR DOCKING SIMULATION; MUTATION, MISSENSE; PROLINE; PROTEIN STRUCTURE, SECONDARY;

EID: 84892918422     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.2317     Document Type: Article

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