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'''Human Carbonic Anhydrase II complexed with two-prong inhibitors''' | '''Human Carbonic Anhydrase II complexed with two-prong inhibitors''' | ||
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[[Category: Christianson, D W.]] | [[Category: Christianson, D W.]] | ||
[[Category: Jude, K M.]] | [[Category: Jude, K M.]] | ||
[[Category: | [[Category: Copper]] | ||
[[Category: | [[Category: Inhibitor]] | ||
[[Category: | [[Category: Lyase]] | ||
[[Category: | [[Category: Zinc]] | ||
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Revision as of 01:09, 4 May 2008
Human Carbonic Anhydrase II complexed with two-prong inhibitors
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
2FOV is a Single protein structure of sequence from Homo sapiens. 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 Page seeded by OCA on Sun May 4 04:09:02 2008
