Modeling of arylamide helix mimetics in the p53 peptide binding site of hDM2 suggests parallel and anti-parallel conformations are both stable

PLoS ONE

Volumn 7, Issue 8, 2012, Pages

  Fuller, Jonathan C ^a,b,c   Jackson, Richard M ^a   Edwards, Thomas A ^a   Wilson, Andrew J ^a   Shirts, Michael R ^b  

^a UNIVERSITY OF LEEDS   (United Kingdom)

^b University of Virginia   (United States)

^c HEIDELBERG INSTITUTE FOR THEORETICAL STUDIES   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

AROMATIC AMIDE; PROTEIN MDM2; PROTEIN P53;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARTICLE; BINDING AFFINITY; BINDING SITE; CARBOXY TERMINAL SEQUENCE; CRYSTALLOGRAPHY; HYDROGEN BOND; HYDROPHOBICITY; MOLECULAR DOCKING; MOLECULAR DYNAMICS; MOLECULAR MODEL; NUCLEAR MAGNETIC RESONANCE; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN PROTEIN INTERACTION; PROTON TRANSPORT; SEQUENCE HOMOLOGY; SIGNAL TRANSDUCTION; SIMULATION;

BINDING SITES; HUMANS; IMIDAZOLES; MOLECULAR DYNAMICS SIMULATION; PEPTIDE FRAGMENTS; PIPERAZINES; PROTO-ONCOGENE PROTEINS C-MDM2; TUMOR SUPPRESSOR PROTEIN P53;

EID: 84865168161     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0043253     Document Type: Article

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