Structure and enzymology of a death-associated protein kinase.
The structure of the catalytic domain of death-associated protein kinase (DAPK), a serine/threonine kinase implicated in programmed cell death and tumor suppression, has been determined recently in several crystal forms, including the highest resolution kinase structure available. The structures provide detailed knowledge about ATP-kinase complexes, reveal novel features that might be important in the regulation of enzyme activity, and allow a proteomics-type approach to DAPK enzymology and its role in signal transduction pathways.
Van Eldik
Linda J
LJ
Drug Discovery Program and Department of Cell and Molecular Biology, Northwestern University Medical School, Chicago IL 60611, USA. vaneldik@northwestern.edu
D000818:Animals; D017209:Apoptosis / Q000502:physiology*; D051017:Apoptosis Regulatory Proteins; D017871:Calcium-Calmodulin-Dependent Protein Kinases / Q000737:chemistry* / Q000378:metabolism*; D064550:Death-Associated Protein Kinases; D006801:Humans; D011487:Protein Conformation
D051017:Apoptosis Regulatory Proteins; D064550:Death-Associated Protein Kinases; D017871:Calcium-Calmodulin-Dependent Protein Kinases