Structural basis for G9a-like protein lysine methyltransferase inhibition by BIX-01294

We present the crystal structure of the catalytic SET domain of G9a-like protein (GLP) in complex with BIX-01294. The inhibitor is bound in the substrate peptide groove at the location where the histone H3 residues (Lys4 to Arg8) N-terminal to the target lysine would occupy. The inhibitor is positio...

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Detalles Bibliográficos
Autores principales: Chang, Yanqi, Zhang, Xing, Horton, John R., Upadhyay, Anup K., Spannhoff, Astrid, Liu, Jin, Snyder, James P., Bedford, Mark T., Cheng, Xiaodong
Formato: Texto
Lenguaje:English
Publicado: 2009
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2676930/
https://www.ncbi.nlm.nih.gov/pubmed/19219047
http://dx.doi.org/10.1038/nsmb.1560
Descripción
Sumario:We present the crystal structure of the catalytic SET domain of G9a-like protein (GLP) in complex with BIX-01294. The inhibitor is bound in the substrate peptide groove at the location where the histone H3 residues (Lys4 to Arg8) N-terminal to the target lysine would occupy. The inhibitor is positioned in place by residues specific for G9a and GLP using planar stacking contacts, polar hydrogen bonds and van der Waals interactions.

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