Protein kinase inhibitor selectivity "hinges" on evolution

Safal Shrestha; George Bendzunas; Natarajan Kannan

doi:10.1016/j.str.2022.11.004

Protein kinase inhibitor selectivity "hinges" on evolution

Structure. 2022 Dec 1;30(12):1561-1563. doi: 10.1016/j.str.2022.11.004.

Authors

Safal Shrestha¹, George Bendzunas², Natarajan Kannan³

Affiliations

¹ Institute of Bioinformatics, University of Georgia, Athens, GA 30602, USA.
² Department of Biochemistry and Molecular Biology, University of Georgia, Athens, GA 30602, USA.
³ Institute of Bioinformatics, University of Georgia, Athens, GA 30602, USA; Department of Biochemistry and Molecular Biology, University of Georgia, Athens, GA 30602, USA. Electronic address: nkannan@uga.edu.

PMID: 36459973
DOI: 10.1016/j.str.2022.11.004

Abstract

In this issue of Structure, Kelso et al. present the crystal structure of the understudied cancer-associated cyclin-dependent kinase 11 (CDK11) bound to the selective inhibitor OTS964, illuminating how evolutionary variations in the kinase domain can be exploited for inhibitor selectivity even among closely related kinases.

Publication types

Research Support, N.I.H., Extramural
Comment

MeSH terms

Antineoplastic Agents*
Protein Kinase Inhibitors* / pharmacology

Substances

Protein Kinase Inhibitors
Antineoplastic Agents

Abstract

Publication types

MeSH terms

Substances

Grants and funding