2fos

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spinqualitylabelsall models 2fos, resolution 1.1Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Human Carbonic Anhydrase II complexed with two-prong inhibitors

Contents 1 Overview 2 Disease 3 About this Structure 4 Reference

Overview

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.

Disease

Known disease associated with this structure: Osteopetrosis, autosomal recessive 3, with renal tubular acidosis OMIM:[611492]

About this Structure

2FOS is a Single protein structure of sequence from Homo sapiens with ZN, CU and B17 as ligands. Active as Carbonate dehydratase, with EC number 4.2.1.1 Full crystallographic information is available from OCA.

Reference

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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