Selectivity by Small-Molecule Inhibitors of Protein Interactions Can Be Driven by Protein Surface Fluctuations

PLoS Computational Biology

Volumn 11, Issue 2, 2015, Pages

  Johnson, David K ^a   Karanicolas, John ^a  

^a UNIVERSITY OF KANSAS   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

LIGANDS; MOLECULES; PROTEINS; SCAFFOLDS (BIOLOGY);

BCL-2 FAMILY PROTEINS; BOUND PROTEINS; PROTEIN FAMILY; PROTEIN INTERACTION; PROTEIN SURFACE; SMALL MOLECULES; SMALL-MOLECULE INHIBITORS; STRUCTURAL STUDIES; SURFACE FLUCTUATIONS; THERAPEUTIC INTERVENTION;

CONFORMATIONS;

PROTEIN BCL 2; PROTEIN BCL XL; PROTEIN MCL 1;

ARTICLE; CRYSTAL STRUCTURE; LIGAND BINDING; PROTEIN CONFORMATION; PROTEIN PROTEIN INTERACTION; SIMULATION; SURFACE PROPERTY; ANIMAL; ANTAGONISTS AND INHIBITORS; BINDING SITE; BIOLOGY; CHEMICAL STRUCTURE; CHEMISTRY; COMPUTER SIMULATION; DRUG DEVELOPMENT; HUMAN; MOUSE; THERMODYNAMICS;

ANIMALS; BINDING SITES; COMPUTATIONAL BIOLOGY; COMPUTER SIMULATION; DRUG DISCOVERY; HUMANS; MICE; MODELS, MOLECULAR; PROTEIN CONFORMATION; PROTO-ONCOGENE PROTEINS C-BCL-2; SURFACE PROPERTIES; THERMODYNAMICS;

EID: 84924390053     PISSN: 1553734X     EISSN: 15537358     Source Type: Journal    
DOI: 10.1371/journal.pcbi.1004081     Document Type: Article

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