ArticleJournal of the American Chemical Society2006
Ultrahigh resolution crystal structures of human carbonic anhydrases I and II complexed with "two-prong" inhibitors reveal the molecular basis of high affinity.
Article in Journal of the American Chemical Society, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 75 citations in OpenAlex.
- PinMyMetal: a hybrid learning system to accurately model transition metal binding sites in macromolecules.Nature communications · 2025Article
- Toxic Metal Species and 'Endogenous' Metalloproteins at the Blood-Organ Interface: Analytical and Bioinorganic Aspects.Molecules (Basel, Switzerland) · 2021Article
- Characterization of the Copper(II) Binding Sites in Human Carbonic Anhydrase II.Inorganic chemistry · 2015Article
- Enantiopure Cryptophane-Supramolecular chemistry · 2015Article
- Article
- Effects of cryoprotectants on the structure and thermostability of the human carbonic anhydrase II-acetazolamide complex.Acta crystallographica. Section D, Biological crystallography · 2013Article
- Insights towards sulfonamide drug specificity in α-carbonic anhydrases.Bioorganic & medicinal chemistry · 2013Article
- Stabilization of anionic and neutral forms of a fluorophoric ligand at the active site of human carbonic anhydrase I.Biochimica et biophysica acta · 2010Article
- Atomic resolution studies of carbonic anhydrase II.Acta crystallographica. Section D, Biological crystallography · 2010Article
- High-resolution structure of human carbonic anhydrase II complexed with acetazolamide reveals insights into inhibitor drug design.Acta crystallographica. Section F, Structural biology and crystallization communications · 2009Article
- Application of metal coordination chemistry to explore and manipulate cell biology.Chemical reviews · 2009Review
- Carbonic anhydrase as a model for biophysical and physical-organic studies of proteins and protein-ligand binding.Chemical reviews · 2008Review
- Structural analysis of charge discrimination in the binding of inhibitors to human carbonic anhydrases I and II.Journal of the American Chemical Society · 2007Article
- Thermodynamic parameters for the association of fluorinated benzenesulfonamides with bovine carbonic anhydrase II.Chemistry, an Asian journal · 2007Article
- Binding of uridine 5'-diphosphate in the "basic patch" of the zinc deacetylase LpxC and implications for substrate binding.Biochemistry · 2006Article
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8 authors at 3 institutions in 1 country.
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Abstract
The atomic-resolution crystal structures of human carbonic anhydrases I and II complexed with "two-prong" inhibitors are reported. Each inhibitor contains a benzenesulfonamide prong and a cupric iminodiacetate (IDA-Cu(2+)) prong separated by linkers of different lengths and compositions. The ionized NH(-) group of each benzenesulfonamide coordinates to the active site Zn(2+) ion; the IDA-Cu(2+) prong of the tightest-binding inhibitor, BR30, binds to H64 of CAII and H200 of CAI. This work provides the first evidence verifying the structural basis of nanomolar affinity measured for two-prong inhibitors targeting the carbonic anhydrases.
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