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肌醇多磷酸5-磷酸酶催化结构域的结构与功能

The structure and function of catalytic domains within inositol polyphosphate 5-phosphatases.

作者信息

Whisstock J C, Wiradjaja F, Waters J E, Gurung R

机构信息

Department of Biochemistry and Molecular Biology, Monash University, Victoria, Australia.

出版信息

IUBMB Life. 2002 Jan;53(1):15-23. doi: 10.1080/15216540210814.

Abstract

Phosphoinositide signaling pathways regulate many essential cellular functions including proliferation, differentiation and survival, cytoskeletal organization, and vesicular trafficking. The inositol polyphosphate 5-phosphatases regulate the cellular levels of several bioactive phosphoinositide species. This review describes the structure and function of the 5-phosphatase and Sac1 catalytic domains of these enzymes. The crystal structure of the 5-phosphatase domain has been solved and shares homology with members of the AP endonuclease family. The phosphoinositide polyphosphatase activity of the Sac1 domain, found in some inositol polyphosphate 5-phosphatases, is defined by a motif, CX5 R(T/S), also found in both protein and lipid phosphatases.

摘要

磷酸肌醇信号通路调节许多重要的细胞功能,包括增殖、分化和存活、细胞骨架组织以及囊泡运输。肌醇多磷酸5-磷酸酶调节几种生物活性磷酸肌醇物种的细胞水平。本综述描述了这些酶的5-磷酸酶和Sac1催化结构域的结构与功能。5-磷酸酶结构域的晶体结构已得到解析,与AP核酸内切酶家族成员具有同源性。在一些肌醇多磷酸5-磷酸酶中发现的Sac1结构域的磷酸肌醇多磷酸酶活性由一个基序CX5R(T/S)定义,该基序也存在于蛋白质和脂质磷酸酶中。

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