TY - JOUR
T1 - The Landscape of Atypical and Eukaryotic Protein Kinases
AU - Kanev, Georgi K.
AU - de Graaf, Chris
AU - de Esch, Iwan J.P.
AU - Leurs, Rob
AU - Würdinger, Thomas
AU - Westerman, Bart A.
AU - Kooistra, Albert J.
PY - 2019/11
Y1 - 2019/11
N2 - Kinases are attractive anticancer targets due to their central role in the growth, survival, and therapy resistance of tumor cells. This review explores the two primary kinase classes, the eukaryotic protein kinases (ePKs) and the atypical protein kinases (aPKs), and provides a structure-centered comparison of their sequences, structures, hydrophobic spines, mutation and SNP hotspots, and inhibitor interaction patterns. Despite the limited sequence similarity between these two classes, atypical kinases commonly share the archetypical kinase fold but lack conserved eukaryotic kinase motifs and possess altered hydrophobic spines. Furthermore, atypical kinase inhibitors explore only a limited number of binding modes both inside and outside the orthosteric binding site. The distribution of genetic variations in both classes shows multiple ways they can interfere with kinase inhibitor binding. This multilayered review provides a research framework bridging the eukaryotic and atypical kinase classes.
AB - Kinases are attractive anticancer targets due to their central role in the growth, survival, and therapy resistance of tumor cells. This review explores the two primary kinase classes, the eukaryotic protein kinases (ePKs) and the atypical protein kinases (aPKs), and provides a structure-centered comparison of their sequences, structures, hydrophobic spines, mutation and SNP hotspots, and inhibitor interaction patterns. Despite the limited sequence similarity between these two classes, atypical kinases commonly share the archetypical kinase fold but lack conserved eukaryotic kinase motifs and possess altered hydrophobic spines. Furthermore, atypical kinase inhibitors explore only a limited number of binding modes both inside and outside the orthosteric binding site. The distribution of genetic variations in both classes shows multiple ways they can interfere with kinase inhibitor binding. This multilayered review provides a research framework bridging the eukaryotic and atypical kinase classes.
KW - catalytic kinase domain structures
KW - eukaryotic and atypical protein kinases
KW - oncogenic mutations
KW - selective kinase inhibitor design
KW - small-molecule kinase inhibitors
KW - SNP
UR - http://www.scopus.com/inward/record.url?scp=85074413986&partnerID=8YFLogxK
U2 - 10.1016/j.tips.2019.09.002
DO - 10.1016/j.tips.2019.09.002
M3 - Review article
C2 - 31677919
AN - SCOPUS:85074413986
VL - 40
SP - 818
EP - 832
JO - Trends in Pharmacological Sciences
JF - Trends in Pharmacological Sciences
SN - 0165-6147
IS - 11
ER -