Structural and functional characterization of the human protein kinase ASK1.

Journal article

Apoptosis signal-regulating kinase 1 (ASK1) plays an essential role in stress and immune response and has been linked to the development of several diseases. Here, we present the structure of the human ASK1 catalytic domain in complex with staurosporine. Analytical ultracentrifugation (AUC) and crystallographic analysis showed that ASK1 forms a tight dimer (K(d) approximately 0.2 microM) interacting in a head-to-tail fashion. We found that the ASK1 phosphorylation motifs differ from known ASK...

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Authors: Bunkoczi, G; Salah, E; Filippakopoulos, P; Fedorov, O; Müller, S

• Journal: Structure (London, England : 1993)
• Volume: 15
• Issue: 10
• Pages: 1215-26
• Publication date: 2007-10-01
• ISSN: 0969-2126
• Language: English
• Subjects: Enzyme Inhibitors; Amino Acid Sequence; chemistry; Humans; Staurosporine; Models, Molecular; Molecular Sequence Data; Phosphorylation; Binding Sites; Protein Conformation; MAP Kinase Kinase Kinase 5; Catalysis; metabolism; Protein Structure, Tertiary; Dimerization; Substrate Specificity; Enzyme Activation; Structure-Activity Relationship