ArticleThe EMBO journal2003
Identification of residues contributing to the ATP binding site of Kir6.2.
Article in The EMBO journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
32 citing papers in PubMed, 79 citations in OpenAlex.
- Electro-metabolic signaling.The Journal of general physiology · 2024Article
- Fine-tuned photochromic sulfonylureas for optical control of beta cell CaDiabetic medicine : a journal of the British Diabetic Association · 2023Article
- Ligand-mediated Structural Dynamics of a Mammalian Pancreatic KJournal of molecular biology · 2022Article
- Control of Kir channel gating by cytoplasmic domain interface interactions.The Journal of general physiology · 2017Article
- Structural Basis for Differences in Dynamics Induced by Leu Versus Ile Residues in the CD Loop of Kir Channels.Molecular neurobiology · 2016Article
- Functional and Modeling Studies of the Transmembrane Region of the TRPM8 Channel.Biophysical journal · 2015Article
- Elucidation of the Inhibitory Effect of Phytochemicals with Kir6.2 Wild-Type and Mutant Models Associated in Type-1 Diabetes through Molecular Docking Approach.Genomics & informatics · 2014Article
- Decomposition of slide helix contributions to ATP-dependent inhibition of Kir6.2 channels.The Journal of biological chemistry · 2013Article
- Regulation of cardiac ATP-sensitive potassium channel surface expression by calcium/calmodulin-dependent protein kinase II.The Journal of biological chemistry · 2013Article
- Regulation of the ATP-sensitive potassium channel subunit, Kir6.2, by a Ca2+-dependent protein kinase C.The Journal of biological chemistry · 2012Article
- Channeling dysglycemia: ion-channel variations perturbing glucose homeostasis.Trends in endocrinology and metabolism: TEM · 2012Review
- Current understanding of K ATP channels in neonatal diseases: focus on insulin secretion disorders.Acta pharmacologica Sinica · 2011Review
- K(ATP) channelopathies in the pancreas.Pflugers Archiv : European journal of physiology · 2010Review
- Muscle KATP channels: recent insights to energy sensing and myoprotection.Physiological reviews · 2010Review
- Identification and characterization of a novel bacterial ATP-sensitive K+ channel.Journal of microbiology (Seoul, Korea) · 2010Article
- Noble gas xenon is a novel adenosine triphosphate-sensitive potassium channel opener.Anesthesiology · 2010Article
- ATP modulation of Ca2+ release by type-2 and type-3 inositol (1, 4, 5)-triphosphate receptors. Differing ATP sensitivities and molecular determinants of action.The Journal of biological chemistry · 2008Article
- How ATP inhibits the open K(ATP) channel.The Journal of general physiology · 2008Article
- ATP-sensitive potassium currents reduce the PGE2-mediated enhancement of excitability in adult rat sensory neurons.Brain research · 2007Article
- Cysteine substitution mutants give structural insight and identify ATP binding and activation sites at P2X receptors.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2007Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The ATP-sensitive potassium (K(ATP)) channel links cell metabolism to membrane excitability. Intracellular ATP inhibits channel activity by binding to the Kir6.2 subunit of the channel, but the ATP binding site is unknown. Using cysteine-scanning mutagenesis and charged thiol-modifying reagents, we identified two amino acids in Kir6.2 that appear to interact directly with ATP: R50 in the N-terminus, and K185 in the C-terminus. The ATP sensitivity of the R50C and K185C mutant channels was increased by a positively charged thiol reagent (MTSEA), and was reduced by the negatively charged reagent MTSES. Comparison of the inhibitory effects of ATP, ADP and AMP after thiol modification suggests that K185 interacts primarily with the beta-phosphate, and R50 with the gamma-phosphate, of ATP. A molecular model of the C-terminus of Kir6.2 (based on the crystal structure of Kir3.1) was constructed and automated docking was used to identify residues interacting with ATP. These results support the idea that K185 interacts with the beta-phosphate of ATP. Thus both N- and C-termini may contribute to the ATP binding site.
Indexed as
Identifiers
What OpenQuestion holds
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.