ArticleThe Journal of biological chemistry2001
Structure of pyruvate dehydrogenase kinase. Novel folding pattern for a serine protein kinase.
Article in The Journal of biological chemistry, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 99 citations in OpenAlex.
- The Pyruvate Dehydrogenase Complex: A 90-Year-Old Enigma Shaping the Future of Structural Enzymology.Advances in experimental medicine and biology · 2026Review
- Investigating Pyruvate Dehydrogenase Kinase 3 Inhibitory Potential of Myricetin Using Integrated Computational and Spectroscopic Approaches.ACS omega · 2024Article
- Natural Product-Based Glycolysis Inhibitors as a Therapeutic Strategy for Epidermal Growth Factor Receptor-Tyrosine Kinase Inhibitor-Resistant Non-Small Cell Lung Cancer.International journal of molecular sciences · 2024Review
- Mitochondrial Alpha-Keto Acid Dehydrogenase Complexes: Recent Developments on Structure and Function in Health and Disease.Sub-cellular biochemistry · 2024Review
- Mitochondrial Kinases and the Role of Mitochondrial Protein Phosphorylation in Health and Disease.Life (Basel, Switzerland) · 2021Review
- Crystal structure of the catalytic subunit of bovine pyruvate dehydrogenase phosphatase.Acta crystallographica. Section F, Structural biology communications · 2020Article
- Discovery of Hordenine as a Potential Inhibitor of Pyruvate Dehydrogenase Kinase 3: Implication in Lung Cancer Therapy.Biomedicines · 2020Article
- Integrative transcriptome, proteome, and microRNA analysis reveals the effects of nitrogen sufficiency and deficiency conditions on theanine metabolism in the tea plant (Horticulture research · 2020Article
- A Structurally-Validated Multiple Sequence Alignment of 497 Human Protein Kinase Domains.Scientific reports · 2019Article
- Structure of the human MLH1 N-terminus: implications for predisposition to Lynch syndrome.Acta crystallographica. Section F, Structural biology communications · 2015Article
- Article
- Regulation of pyruvate metabolism and human disease.Cellular and molecular life sciences : CMLS · 2014Review
- The pyruvate dehydrogenase complexes: structure-based function and regulation.The Journal of biological chemistry · 2014Review
- Structure-guided development of specific pyruvate dehydrogenase kinase inhibitors targeting the ATP-binding pocket.The Journal of biological chemistry · 2014Article
- Pyruvate Dehydrogenase Kinases in the Nervous System: Their Principal Functions in Neuronal-glial Metabolic Interaction and Neuro-metabolic Disorders.Current neuropharmacology · 2012Article
- Inactivation of pyruvate dehydrogenase kinase 2 by mitochondrial reactive oxygen species.The Journal of biological chemistry · 2012Article
- Comparative homology modeling of pyruvate dehydrogenase kinase isozymes from Xenopus tropicalis reveals structural basis for their subfunctionalization.Journal of molecular modeling · 2012Article
- Pivotal role of the C-terminal DW-motif in mediating inhibition of pyruvate dehydrogenase kinase 2 by dichloroacetate.The Journal of biological chemistry · 2009Article
- Subunit and catalytic component stoichiometries of an in vitro reconstituted human pyruvate dehydrogenase complex.The Journal of biological chemistry · 2009Article
- Pyruvate dehydrogenase kinase-4 structures reveal a metastable open conformation fostering robust core-free basal activity.The Journal of biological chemistry · 2008Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
The structure of mitochondrial pyruvate dehydrogenase kinase isozyme 2 is of interest because it represents a family of serine-specific protein kinases that lack sequence similarity with all other eukaryotic protein kinases. Similarity exists instead with key motifs of prokaryotic histidine protein kinases and a family of eukaryotic ATPases. The 2.5-A crystal structure reported here reveals that pyruvate dehydrogenase kinase isozyme 2 has two domains of about the same size. The N-terminal half is dominated by a bundle of four amphipathic alpha-helices, whereas the C-terminal half is folded into an alpha/beta sandwich that contains the nucleotide-binding site. Analysis of the structure reveals this C-terminal domain to be very similar to the nucleotide-binding domain of bacterial histidine kinases, but the catalytic mechanism appears similar to that of the eukaryotic serine kinases and ATPases.
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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.