ArticleProtein science : a publication of the Protein Society2009
Structure of dystrophia myotonica protein kinase.
Article in Protein science : a publication of the Protein Society, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 22 citations in OpenAlex.
- Genome-wide DNA methylation and transcriptome sequencing analyses of lens tissue in an age-related mouse cataract model.PloS one · 2025Article
- Bisindolyl Maleimides and Indolylmaleimide Derivatives-A Review of Their Synthesis and Bioactivity.Pharmaceuticals (Basel, Switzerland) · 2023Review
- A critical evaluation of protein kinase regulation by activation loop autophosphorylation.eLife · 2023Article
- Review
- Revealing phosphorylation regulatory networks during embryogenesis of honey bee worker and drone (Frontiers in cell and developmental biology · 2022Article
- Made to measure - keeping Rho kinase at a distance.Small GTPases · 2016Review
- Myotonic dystrophy kinase-related Cdc42-binding kinases (MRCK), the ROCK-like effectors of Cdc42 and Rac1.Small GTPases · 2015Review
- Molecular basis for the fold organization and sarcomeric targeting of the muscle atrogin MuRF1.Open biology · 2014Article
- The actin-myosin regulatory MRCK kinases: regulation, biological functions and associations with human cancer.Journal of molecular medicine (Berlin, Germany) · 2014Review
- Rho-associated coiled-coil containing kinases (ROCK): structure, regulation, and functions.Small GTPases · 2014Review
- Co-crystal structures of inhibitors with MRCKβ, a key regulator of tumor cell invasion.PloS one · 2011Article
- Biophysical characterization of recombinant proteins: a key to higher structural genomics success.Journal of structural biology · 2010Review
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Dystrophia myotonica protein kinase (DMPK) is a serine/threonine kinase composed of a kinase domain and a coiled-coil domain involved in the multimerization. The crystal structure of the kinase domain of DMPK bound to the inhibitor bisindolylmaleimide VIII (BIM-8) revealed a dimeric enzyme associated by a conserved dimerization domain. The affinity of dimerisation suggested that the kinase domain alone is insufficient for dimerisation in vivo and that the coiled-coil domains are required for stable dimer formation. The kinase domain is in an active conformation, with a fully-ordered and correctly positioned alphaC helix, and catalytic residues in a conformation competent for catalysis. The conserved hydrophobic motif at the C-terminal extension of the kinase domain is bound to the N-terminal lobe of the kinase domain, despite being unphosphorylated. Differences in the arrangement of the C-terminal extension compared to the closely related Rho-associated kinases include an altered PXXP motif, a different conformation and binding arrangement for the turn motif, and a different location for the conserved NFD motif. The BIM-8 inhibitor occupies the ATP site and has similar binding mode as observed in PDK1.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.