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Article

Site-directed mutagenesis of the glycine-rich loop of death associated protein kinase (DAPK) identifies it as a key structure for catalytic activity.

Biochimica et biophysica acta - 1 May 2011

McNamara Laurie K, Brunzelle Joseph S, Schavocky James P, Watterson D Martin, Grum-Tokars Valerie

Abstract excerpt

Death associated protein kinase (DAPK) is a calmodulin (CaM)-regulated protein kinase that is a therapeutic target for central nervous system (CNS) disorders. We report here the results of studies that test the hypothesis of McNamara et al. (2009) that conformational selection in DAPK's glycine-rich region is key for catalytic activity. The hypothesis was tested by site-directed mutagenesis of glutamine-23 (Q23)...

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Identifiers

PMID: 21126544
DOI: 10.1016/j.bbamcr.2010.11.011
PMCID: PMC3101106

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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