Identification of the binding site of an allosteric ligand using STD-NMR, docking, and CORCEMA-ST calculations.

Zhang, Wei; Li, Rongbao; Shin, Ronald; Wang, Yimin; Padmalayam, Indira; Zhai, Ling; Krishna, N Rama

Zhang, Wei; Li, Rongbao; Shin, Ronald; Wang, Yimin; Padmalayam, Indira; Zhai, Ling; Krishna, N Rama.

Affiliation

Zhang W; Drug Discovery Division, Southern Research Institute, 2000 9th Avenue South, Birmingham, AL 35205 (USA). zhangw@sri.org.

ChemMedChem ; 8(10): 1629-33, 2013 Oct.

Article in En | MEDLINE | ID: mdl-23894090

ABSTRACT

ABSTRACT

Singling out the truth A combined application of STD-NMR, molecular docking, and CORCEMA-ST calculations is described as an attractive, easily applicable tool for the identification and validation of the binding site for allosteric ligands, with potential application as an aid in drug discovery research.

Subject(s)

Ligands; Molecular Docking Simulation; Nuclear Magnetic Resonance, Biomolecular; Allosteric Regulation; Binding Sites; Humans; Kinesins/chemistry; Kinesins/metabolism; Kinetics; Protein Binding; Protein Structure, Tertiary

Key words

CORCEMAST; STDNMR; allosteric binding sites; drug discovery; kinesin Eg5

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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Nuclear Magnetic Resonance, Biomolecular / Molecular Docking Simulation / Ligands Type of study: Diagnostic_studies Limits: Humans Language: En Journal: ChemMedChem Journal subject: FARMACOLOGIA / QUIMICA Year: 2013 Document type: Article

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