ArticleActa crystallographica. Section D, Biological crystallography2014
Structural elucidation of the hormonal inhibition mechanism of the bile acid cholate on human carbonic anhydrase II.
Article in Acta crystallographica. Section D, Biological crystallography, 2014. 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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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
8 citing papers in PubMed, 22 citations in OpenAlex.
- Purification, Characterization, cDNA Cloning, and Bioinformatic Analysis of Zinc-Binding Protein fromMolecules (Basel, Switzerland) · 2024Article
- Assessment of the risk factors of duodenogastric reflux in relation to different dietary habits in a Chinese population of the Zhangjiakou area.Food & nutrition research · 2023Article
- Ibuprofen: a weak inhibitor of carbonic anhydrase II.Acta crystallographica. Section F, Structural biology communications · 2022Article
- Carbonic Anhydrases II, IX, and XII in Reflux Esophagitis.Digestive diseases and sciences · 2022Article
- Transcriptome Profiling of Placenta through Pregnancy Reveals Dysregulation of Bile Acids Transport and Detoxification Function.International journal of molecular sciences · 2019Article
- Carbonic anhydrase II in complex with carboxylic acid-based inhibitors.Acta crystallographica. Section F, Structural biology communications · 2019Article
- Steroids interfere with human carbonic anhydrase activity by using alternative binding mechanisms.Journal of enzyme inhibition and medicinal chemistry · 2018Article
- Bile Acid Conjugated DNA Chimera that Conditionally Inhibits Carbonic Anhydrase-II in the Presence of MicroRNA-21.Bioconjugate chemistry · 2015Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The carbonic anhydrases (CAs) are a family of mostly zinc metalloenzymes that catalyze the reversible hydration/dehydration of CO2 into bicarbonate and a proton. Human isoform CA II (HCA II) is abundant in the surface epithelial cells of the gastric mucosa, where it serves an important role in cytoprotection through bicarbonate secretion. Physiological inhibition of HCA II via the bile acids contributes to mucosal injury in ulcerogenic conditions. This study details the weak biophysical interactions associated with the binding of a primary bile acid, cholate, to HCA II. The X-ray crystallographic structure determined to 1.54 Å resolution revealed that cholate does not make any direct hydrogen-bond interactions with HCA II, but instead reconfigures the well ordered water network within the active site to promote indirect binding to the enzyme. Structural knowledge of the binding interactions of this nonsulfur-containing inhibitor with HCA II could provide the template design for high-affinity, isoform-specific therapeutic agents for a variety of diseases/pathological states, including cancer, glaucoma, epilepsy and osteoporosis.
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