Membrane Interaction and Functional Plasticity of Inositol Polyphosphate 5-Phosphatases

被引:8
作者
Braun, Werner [1 ,2 ]
Schein, Catherine H. [3 ]
机构
[1] Univ Texas Med Branch, Sealy Ctr Struct Biol & Mol Biophys, Galveston, TX 77555 USA
[2] Univ Texas Med Branch, Dept Biochem & Mol Biol, Galveston, TX 77555 USA
[3] Fdn Appl Mol Evolut, Gainesville, FL 32601 USA
关键词
DNA-REPAIR; ENDONUCLEASES; SPECIFICITY; CATALYSIS; MECHANISM; BINDING; APE1;
D O I
10.1016/j.str.2014.04.008
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
In this issue of Structure, Tresaugues and colleagues determined the interaction of membrane-bound phosphoinositides with three clinically significant human inositol polyphosphate 5-phosphatases (I5Ps). A comparison to the structures determined with soluble substrates revealed differences in the binding mode and suggested how the I5Ps and apurinic endonuclease (APE1) activities evolved from the same metal-binding active center.
引用
收藏
页码:664 / 666
页数:4
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