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HDX-MS Analysis of CHK2 Incubated with Calmodulin

ABSTRACT: To determine the conformational dynamics upon binding of calmodulin to serine/threonine kinase CHK2.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: John Burke

LAB HEAD: Dr. John E. Burke

PROVIDER: PXD048473 | Pride | 2025-10-15

REPOSITORIES: Pride

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Dataset's files

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			Action	DRS
	10_17_23_HNHDX2_HK_MSMS.d.rar	Other
	11_21_23_HN7_HK_ND.d.rar	Other
	11_22_23_HN7_CC_30s-1.d.rar	Other
	11_22_23_HN7_HK_30s-1.d.rar	Other
	11_23_23_HN7_CC_300s-1.d.rar	Other

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1 - 5 of 39

Publications

Unconventional binding of calmodulin to CHK2 kinase inhibits catalytic activity.

Horne Christopher R CR Wang Tingting T Young Samuel N SN Dite Toby A TA Nyvall Hunter G HG Suresh Sushant S Davies Katherine A KA Gonzalez Castro Abner A Vaibhav Vineet V Mather Lucy J LJ Dagley Laura F LF Belousoff Matthew J MJ Manning Gerard G Means Anthony R AR Burke John E JE Petersen Janni J Scott John W JW Murphy James M JM

The Biochemical journal 20251201 23

Calmodulin (CaM) serves an essential role in eukaryotic cells as a Ca2+ sensor. Ca2+ binding leads to conformation changes in CaM that enable engagement of a repertoire of enzymes and the regulation of their catalytic activities. Classically, Ca2+-CaM binds to an inhibitory pseudosubstrate sequence C-terminal to the kinase domain in members of the Ca2+-CaM-dependent protein kinase (CAMK) family and relieves inhibition to promote catalytic activity. Here, we report an unexpected mechanism by whic ...[more]

PMID: 41003242

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