KA1 Domains: Unity in Mechanistic Diversity

YiTing Paung; Markus A Seeliger

doi:10.1016/j.str.2018.07.002

KA1 Domains: Unity in Mechanistic Diversity

Structure. 2018 Aug 7;26(8):1045-1047. doi: 10.1016/j.str.2018.07.002.

Authors

YiTing Paung¹, Markus A Seeliger²

Affiliations

¹ Department of Pharmacological Sciences, Stony Brook University, School of Medicine, BST 8-140, Stony Brook, NY 11794, USA.
² Department of Pharmacological Sciences, Stony Brook University, School of Medicine, BST 8-140, Stony Brook, NY 11794, USA. Electronic address: markus.seeliger@stonybrook.edu.

PMID: 30089246
DOI: 10.1016/j.str.2018.07.002

Abstract

The enzymatic activity of protein kinases is often tightly controlled by regulatory domains with a conserved structural mechanism. In this issue of Structure, Emptage et al. (2018) report how the kinase associated-1 domain (KA1) autoinhibits kinase activity with a striking structural diversity.

Publication types

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

MeSH terms

Amino Acid Sequence
Models, Molecular
Phosphorylation
Protein Kinases*

Substances

Protein Kinases

Grants and funding

R35 GM119437/GM/NIGMS NIH HHS/United States