Backbone resonance assignments of the catalytic and regulatory domains of Ca2+/calmodulin-dependent protein kinase 1D

Michael H G Tong; Mark Jeeves; Sundaresan Rajesh; Christian Ludwig; Marc Lenoir; Jitendra Kumar; Darren M McClelland; Fedor Berditchevski; Julia A Hubbard; Colin Kenyon; Sam Butterworth; Stefan Knapp; Michael Overduin

doi:10.1007/s12104-020-09950-x

Backbone resonance assignments of the catalytic and regulatory domains of Ca²⁺/calmodulin-dependent protein kinase 1D

Biomol NMR Assign. 2020 Oct;14(2):221-225. doi: 10.1007/s12104-020-09950-x. Epub 2020 Jun 13.

Affiliations

¹ Institute of Cancer and Genomic Sciences, University of Birmingham, Edgbaston, Birmingham, B15 2TT, UK.
² Department of Biochemistry, University of Alberta, Edmonton, AB, T6G 2H7, Canada.
³ Computational, Analytical and Structural Sciences, GlaxoSmithKline, Gunnels Wood Road, Stevenage, Hertfordshire, SG1 2NY, UK.
⁴ Faculty of Medicine and Health Sciences, Stellenbosch University, Francie Van Zijl Dr, Parow, Cape Town, 7505, South Africa.
⁵ Division of Pharmacy and Optometry, School of Health Sciences, Manchester Academic Health Sciences Centre, University of Manchester, Manchester, M13 9PL, UK.
⁶ Structural Genomics Consortium and Buchmann Institute for Molecular Life Sciences, Institute for Pharmaceutical Chemistry, Johann Wolfgang Goethe-University, Max-von-Laue-Straße 9, 60438, Frankfurt am Main, Germany.
⁷ Department of Biochemistry, University of Alberta, Edmonton, AB, T6G 2H7, Canada. [email protected].

Abstract

The CaMK subfamily of Ser/Thr kinases are regulated by calmodulin interactions with their C-terminal regions. They are exemplified by Ca²⁺/calmodulin dependent protein kinase 1δ which is known as CaMK1D, CaMKIδ or CKLiK. CaMK1D mediates intracellular signalling downstream of Ca²⁺ influx and thereby exhibits amplifications of Ca²⁺signals and polymorphisms that have been implicated in breast cancer and diabetes. Here we report the backbone ¹H, ¹³C, ¹⁵N assignments of the 38 kDa human CaMK1D protein in its free state, including both the canonical bi-lobed kinase fold as well as the autoinhibitory and calmodulin binding domains.

Keywords: CKLiK; CaMK1D; CaMKIδ; Calcium/calmodulin dependent protein kinase; NMR; Protein resonance assignment.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Amino Acid Sequence
Biocatalysis*
Calcium-Calmodulin-Dependent Protein Kinase Type 1 / chemistry*
Humans
Nuclear Magnetic Resonance, Biomolecular*
Protein Domains
Protein Structure, Secondary

Substances

CAMK1D protein, human
Calcium-Calmodulin-Dependent Protein Kinase Type 1