Crystal structure of human nucleoside diphosphate kinase A, a metastasis suppressor
Crystal structure of human nucleoside diphosphate kinase A, a metastasis suppressor
复制标题
转移抑制剂人核苷二磷酸激酶 A 的晶体结构
DOI：
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发表时间：
2002
期刊：
影响因子：
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通讯作者：
S. Suh
中科院分区：
文献类型：
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作者：
K. Min;H. Song;Changsoo Chang;Sun Kim;Kong;S. Suh
导论.核苷二磷酸激酶（NDK）通过使用ATP作为主要磷酸供体催化g-磷酰基从核苷三磷酸（NTP）转移到核苷二磷酸（NDP）。在催化反应期间，酶在保守的组氨酸残基上瞬时磷酸化。NDP激酶在维持所有NTP的细胞库中起主要作用，但也在重要细胞过程的调节中起主要作用。在人类中，两种亚型NDK-A（NM 23-H1）和NDK-B（NM 23-H2）在氨基酸序列上密切相关（88%同一性），但在细胞功能上显示出显著差异。NDK-A作为某些肿瘤类型的转移抑制因子。NDK-B，也称为PuF，与c-myc癌基因的启动子结合并激活其转录。两种亚型的这些细胞功能与它们的NDP激酶活性无关，并且两种亚型可以形成同源和异源六聚体，导致各自亚基的不同比例。我们在这里提出的晶体结构的人NDK-A确定在2.2 μ m分辨率。这使得NDK-A与NDK-B的详细结构比较成为可能，有助于理解其细胞功能的差异。
Introduction. Nucleoside diphosphate kinase (NDK) catalyzes the transfer of the g-phosphoryl group from a nucleoside triphosphate (NTP) to a nucleoside diphosphate (NDP) by using ATP as a major phosphate donor. During the catalytic reaction, the enzyme is transiently phosphorylated on a conserved histidine residue. NDP kinases play a primary role in maintaining cellular pools of all NTPs but also in the regulation of important cellular processes. In humans, the two isoforms NDK-A (NM23-H1) and NDK-B (NM23-H2) are closely related in amino acid sequence (88% identity) but display significant differences in cellular functions. NDK-A acts as a metastasis suppressor for some tumor types. NDK-B, also known as PuF, binds to the promoter of the c-myc oncogene and activates its transcription. These cellular functions of the two isoforms are independent of their NDP kinase activity, and two isoforms can form homoand heterohexamers, resulting in different ratios of the respective subunits. We present here the crystal structure of human NDK-A determined at 2.2 Å resolution. This enables a detailed structural comparison of NDK-A with NDK-B, contributing to understanding the difference in their cellular functions.
影响因子：
5.6
作者：
Philip A. Webb;O. Perisic;Chairmaine E. Mendola;J. Backer;Roger L. Williams
通讯作者：
Philip A. Webb;O. Perisic;Chairmaine E. Mendola;J. Backer;Roger L. Williams