期刊
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
卷 128, 期 9, 页码 3011-3018出版社
AMER CHEMICAL SOC
DOI: 10.1021/ja057257n
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资金
- NCRR NIH HHS [P41 RR001646, RR 01646] Funding Source: Medline
- NIGMS NIH HHS [GM 49758, R01 GM049758-12, R01 GM049758, DMR0225180] Funding Source: Medline
The atomic-resolution crystal structures of human carbonic anhydrases I and I I complexed with two-prong inhibitors are reported. Each inhibitor contains a benzenesulfonamide prong and a cupric iminodiacetate (IDA-Cu2+) prong separated by linkers of different lengths and compositions. The ionized NH- group of each benzenesulfonamide coordinates to the active site Zn2+ ion; the IDA-Cu2+ 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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