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

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

Research output: Contribution to journal › Article › peer-review

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.

Original language	English
Pages (from-to)	221-225
Number of pages	5
Journal	Biomolecular NMR assignments
Volume	14
Issue number	2
DOIs	https://doi.org/10.1007/s12104-020-09950-x
Publication status	Published - Oct 2020

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

SDG 3 Good Health and Well-being

Keywords

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

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Tong, M. H. G., Jeeves, M., Rajesh, S., Ludwig, C., Lenoir, M., Kumar, J., McClelland, D. M., Berditchevski, F., Hubbard, J. A., Kenyon, C., Butterworth, S., Knapp, S., & Overduin, M. (2020). Backbone resonance assignments of the catalytic and regulatory domains of Ca2+/calmodulin-dependent protein kinase 1D. Biomolecular NMR assignments, 14(2), 221-225. https://doi.org/10.1007/s12104-020-09950-x

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

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

author = "Tong, \{Michael H G\} and Mark Jeeves and Sundaresan Rajesh and Christian Ludwig and Marc Lenoir and Jitendra Kumar and McClelland, \{Darren M\} and Fedor Berditchevski and Hubbard, \{Julia A\} and Colin Kenyon and Sam Butterworth and Stefan Knapp and Michael Overduin",

year = "2020",

month = oct,

doi = "10.1007/s12104-020-09950-x",

language = "English",

volume = "14",

pages = "221--225",

journal = "Biomolecular NMR assignments",

issn = "1874-270X",

publisher = "Springer",

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Tong, MHG, Jeeves, M, Rajesh, S, Ludwig, C, Lenoir, M, Kumar, J, McClelland, DM, Berditchevski, F, Hubbard, JA, Kenyon, C, Butterworth, S, Knapp, S & Overduin, M 2020, 'Backbone resonance assignments of the catalytic and regulatory domains of Ca2+/calmodulin-dependent protein kinase 1D', Biomolecular NMR assignments, vol. 14, no. 2, pp. 221-225. https://doi.org/10.1007/s12104-020-09950-x

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T1 - Backbone resonance assignments of the catalytic and regulatory domains of Ca2+/calmodulin-dependent protein kinase 1D

AU - Tong, Michael H G

AU - Jeeves, Mark

AU - Rajesh, Sundaresan

AU - Ludwig, Christian

AU - Lenoir, Marc

AU - Kumar, Jitendra

AU - McClelland, Darren M

AU - Berditchevski, Fedor

AU - Hubbard, Julia A

AU - Kenyon, Colin

AU - Butterworth, Sam

AU - Knapp, Stefan

AU - Overduin, Michael

PY - 2020/10

Y1 - 2020/10

N2 - 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.

AB - 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.

KW - Amino Acid Sequence

KW - Biocatalysis

KW - Calcium-Calmodulin-Dependent Protein Kinase Type 1/chemistry

KW - Humans

KW - Nuclear Magnetic Resonance, Biomolecular

KW - Protein Domains

KW - Protein Structure, Secondary

U2 - 10.1007/s12104-020-09950-x

DO - 10.1007/s12104-020-09950-x

M3 - Article

C2 - 32535836

SN - 1874-270X

VL - 14

SP - 221

EP - 225

JO - Biomolecular NMR assignments

JF - Biomolecular NMR assignments

IS - 2

ER -

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

Abstract

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Keywords

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