Crystal structures of human RIP2 kinase catalytic domain complexed with ATP-competitive inhibitors: Foundations for understanding inhibitor selectivity

[Display omitted] Receptor interacting protein 2 (RIP2) is an intracellular kinase and key signaling partner for the pattern recognition receptors NOD1 and NOD2 (nucleotide-binding oligomerization domain-containing proteins 1 and 2). As such, RIP2 represents an attractive target to probe the role of...

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Veröffentlicht in:	Bioorganic & medicinal chemistry 2015-11, Vol.23 (21), p.7000-7006
Hauptverfasser:	Charnley, Adam K., Convery, Máire A., Lakdawala Shah, Ami, Jones, Emma, Hardwicke, Philip, Bridges, Angela, Ouellette, Michael, Totoritis, Rachel, Schwartz, Benjamin, King, Bryan W., Wisnoski, David D., Kang, James, Eidam, Patrick M., Votta, Bartholomew J., Gough, Peter J., Marquis, Robert W., Bertin, John, Casillas, Linda
Format:	Artikel
Sprache:	eng
Schlagworte:	Adenosine Triphosphate - analogs & derivatives Adenosine Triphosphate - metabolism Binding Sites CARD3 CARDIAK Catalytic Domain Crystallography, X-Ray Drug Design Humans Inhibitor selectivity Inhibitory Concentration 50 Kinase inhibitor Kinase structure Kinetics Molecular Dynamics Simulation Protein Kinase Inhibitors - chemistry Protein Kinase Inhibitors - metabolism Receptor-Interacting Protein Serine-Threonine Kinase 2 - chemistry Receptor-Interacting Protein Serine-Threonine Kinase 2 - metabolism RICK RIP2 RIPK2 Structure-based drug design X-ray cocrystal structure
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