Neutron diffraction of acetazolamide-bound human carbonic anhydrase II reveals atomic details of drug binding.
作者： S. Zoë Fisher , Mayank Aggarwal , Andrey Y. Kovalevsky , David N. Silverman , Robert McKenna
DOI: 10.1021/JA3068098
关键词: Proton 、 Neutron diffraction 、 Hydrogen bond 、 Chemistry 、 Molecule 、 Crystallography 、 Drug design 、 Stereochemistry 、 Binding site 、 Carbonic anhydrase II 、 Sulfonamide
摘要: Carbonic anhydrases (CAs) catalyze the hydration of CO2 forming HCO3– and a proton, an important reaction for many physiological processes including respiration, fluid secretion, pH regulation. As such, CA isoforms are prominent clinical targets treating various diseases. The clinically used acetazolamide (AZM) is sulfonamide that binds with high affinity to human isoform II (HCA II). There several X-ray structures available AZM bound isoforms, but these complexes do not show charged state or hydrogen atom positions protein solvent. Neutron diffraction useful technique directly observing H atoms mapping H-bonding networks can greatly contribute rational drug design. To this end, neutron structure H/D exchanged HCA II crystals in complex was determined. reveals molecular details binding drug. This represents first determined structur...
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