一种新型的人碳酸酐酶II的乙酸盐结合复合物。
A novel acetate-bound complex of human carbonic anhydrase II.
作者信息
Mazumdar Pooja Anjali, Kumaran Desigan, Swaminathan Subramanyam, Das Amit Kumar
机构信息
Department of Biotechnology, Indian Institute of Technology Kharagpur, Kharagpur 721302, India.
出版信息
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Mar 1;64(Pt 3):163-6. doi: 10.1107/S1744309108002078. Epub 2008 Feb 23.
The enzyme human carbonic anhydrase II (hCAII) crystallized in an acetate-bound complex belonging to space group P2(1)2(1)2(1), with unit-cell parameters a = 42.3, b = 71.8, c = 74.0 A. The structure was solved by the molecular-replacement method and refined to an R value of 0.18 and an R(free) of 0.21. The acetate molecule replaced the zinc-bound water molecule in the structure, differing from previous reports regarding the site of acetate binding. This mode of binding disrupts the hydrogen-bonded solvent network required for activity of the enzyme. This mode of inhibitor binding is a novel one that has not been observed previously.
人碳酸酐酶II（hCAII）在属于空间群P2(1)2(1)2(1)的乙酸盐结合复合物中结晶，晶胞参数为a = 42.3、b = 71.8、c = 74.0 Å。该结构通过分子置换法解析，精修后R值为0.18，自由R值为0.21。在该结构中，乙酸盐分子取代了与锌结合的水分子，这与之前关于乙酸盐结合位点的报道不同。这种结合模式破坏了酶活性所需的氢键溶剂网络。这种抑制剂结合模式是一种以前未观察到的新模式。
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