ArticleProceedings of the National Academy of Sciences of the United States of America1998
Conserved water molecules contribute to the extensive network of interactions at the active site of protein kinase A.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
25 citing papers in PubMed, 76 citations in OpenAlex.
- A PKA-selective inhibitor captures an open but more ordered conformation of the PKA catalytic subunit.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Diversification in the inositol tris/tetrakisphosphate kinase (ITPK) family: crystal structure and enzymology of the outlier AtITPK4.The Biochemical journal · 2023Article
- Insights to the Structural Basis for the Stereospecificity of theInternational journal of molecular sciences · 2022Article
- Zooming in on protons: Neutron structure of protein kinase A trapped in a product complex.Science advances · 2019Article
- Towards simple kinetic models of functional dynamics for a kinase subfamily.Nature chemistry · 2018Article
- Water-mediated conformational preselection mechanism in substrate binding cooperativity to protein kinase A.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Effects of protein-crystal hydration and temperature on side-chain conformational heterogeneity in monoclinic lysozyme crystals.Acta crystallographica. Section D, Structural biology · 2018Article
- Atomic Structure of GRK5 Reveals Distinct Structural Features Novel for G Protein-coupled Receptor Kinases.The Journal of biological chemistry · 2015Article
- Molecular features of product release for the PKA catalytic cycle.Biochemistry · 2015Article
- Dynamic architecture of a protein kinase.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Phosphoryl transfer by protein kinase A is captured in a crystal lattice.Journal of the American Chemical Society · 2013Article
- Molecular interactions of c-ABL mutants in complex with imatinib/nilotinib: a computational study using linear interaction energy (LIE) calculations.Journal of molecular modeling · 2012Article
- The role of conserved waters in conformational transitions of Q61H K-ras.PLoS computational biology · 2012Article
- Molecular docking and QSAR of aplyronine A and analogues: potent inhibitors of actin.Journal of computer-aided molecular design · 2010Article
- A transition path ensemble study reveals a linchpin role for Mg(2+) during rate-limiting ADP release from protein kinase A.Biochemistry · 2009Article
- Article
- Structural coupling between FKBP12 and buried water.Proteins · 2009Article
- Synthesis of urea picket porphyrins and their use in the elucidation of the role buried solvent plays in the selectivity and stoichiometry of anion binding receptors.The Journal of organic chemistry · 2007Article
- Release of ADP from the catalytic subunit of protein kinase A: a molecular dynamics simulation study.Protein science : a publication of the Protein Society · 2005Article
- Incorporation of the fluorescent amino acid 7-azatryptophan into the core domain 1-47 of hirudin as a probe of hirudin folding and thrombin recognition.Protein science : a publication of the Protein Society · 2004Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
Abstract
Protein kinases constitute a large family of regulatory enzymes, each with a distinct specificity to restrict its action to its physiological target(s) only. The catalytic (C) subunit of protein kinase A, regarded as a structural prototype for this family, is composed of a conserved core flanked by two nonconserved segments at the amino and carboxyl termini. Here we summarize evidence to show that (i) the active site consists of an extended network of interactions that weave together both domains of the core as well as both segments that flank the core; (ii) the opening and closing of the active site cleft, including the dynamic and coordinated movement of the carboxyl terminal tail, contributes directly to substrate recognition and catalysis; and (iii) in addition to peptide and ATP, the active site contains six structured water molecules that constitute a conserved structural element of the active site. One of these active-site conserved water molecules is locked into place by its interactions with the nucleotide, the peptide substrate/inhibitor, the small and large domains of the conserved core, and Tyr-330 from the carboxyl-terminal "tail."
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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.