TY - JOUR
T1 - Structure and enzymology of a death-associated protein kinase
AU - Van Eldik, Linda J.
PY - 2002/7/1
Y1 - 2002/7/1
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0036640251&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0036640251&partnerID=8YFLogxK
U2 - 10.1016/S0165-6147(02)02049-7
DO - 10.1016/S0165-6147(02)02049-7
M3 - Review article
C2 - 12119143
AN - SCOPUS:0036640251
SN - 0165-6147
VL - 23
SP - 302
EP - 304
JO - Trends in Pharmacological Sciences
JF - Trends in Pharmacological Sciences
IS - 7
ER -