ArticleProtein science : a publication of the Protein Society2010
High-resolution crystal structure of human Mapkap kinase 3 in complex with a high affinity ligand.
Article in Protein science : a publication of the Protein Society, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 18 citations in OpenAlex.
- Dual therapeutic potential of Scoparia dulcis in combating hyperglycemia and inflammation in diabetes through network pharmacology and in silico analysis.Scientific reports · 2025Article
- Network Pharmacology, Molecular Docking and Molecular Dynamics to Explore the Potential Immunomodulatory Mechanisms of Deer Antler.International journal of molecular sciences · 2023Article
- Adaptive Cartesian and torsional restraints for interactive model rebuilding.Acta crystallographica. Section D, Structural biology · 2021Article
- Chrysophanol, Physcion, Hesperidin and Curcumin Modulate the Gene Expression of Pro-Inflammatory Mediators Induced by LPS in HepG2: In Silico and Molecular Studies.Antioxidants (Basel, Switzerland) · 2019Article
- MAPKAPK2: the master regulator of RNA-binding proteins modulates transcript stability and tumor progression.Journal of experimental & clinical cancer research : CR · 2019Review
- Comparative molecular dynamics simulations of mitogen-activated protein kinase-activated protein kinase 5.International journal of molecular sciences · 2014Article
- Homology modeling and ligand docking of Mitogen-activated protein kinase-activated protein kinase 5 (MK5).Theoretical biology & medical modelling · 2013Article
- The diterpenoid alkaloid noroxoaconitine is a Mapkap kinase 5 (MK5/PRAK) inhibitor.Cellular and molecular life sciences : CMLS · 2011Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Mapkap kinases 2 and 3 (MK2 and MK3) have been implicated in intracellular signaling pathways leading to the production of the pro-inflammatory cytokine tumor necrosis factor alpha. MK2 has been pursued by the biopharmaceutical industry for many years for the development of a small molecule anti-inflammatory treatment and drug-like inhibitors have been described. The development of some of these compounds, however, has been slowed by the absence of a high-resolution crystal structure of MK2. Herein we present a high-resolution (1.9 A) crystal structure of the highly homologous MK3 in complex with a pharmaceutical lead compound. While all of the canonical features of Ser/Thr kinases in general and MK2 in particular are recapitulated in MK3, the detailed analysis of the binding interaction of the drug-like ligand within the adenine binding pocket allows relevant conclusions to be drawn for the further design of potent and selective drug candidates.
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