2fov
Human Carbonic Anhydrase II complexed with two-prong inhibitors
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OverviewOverview
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.
DiseaseDisease
Known disease associated with this structure: Osteopetrosis, autosomal recessive 3, with renal tubular acidosis OMIM:[611492]
About this StructureAbout this Structure
2FOV is a Single protein structure of sequence from Homo sapiens with ZN, CU, B30 and CCN as ligands. Active as Carbonate dehydratase, with EC number 4.2.1.1 Full crystallographic information is available from OCA.
ReferenceReference
Ultrahigh resolution crystal structures of human carbonic anhydrases I and II complexed with "two-prong" inhibitors reveal the molecular basis of high affinity., Jude KM, Banerjee AL, Haldar MK, Manokaran S, Roy B, Mallik S, Srivastava DK, Christianson DW, J Am Chem Soc. 2006 Mar 8;128(9):3011-8. PMID:16506782
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