Crystal Structures of Human CaMKI alpha Reveal Insights into the Regulation Mechanism of CaMKI
文献类型:期刊论文
作者 | Zha, MW; Zhong, C; Ou, Y; Han, L; Wang, JC; Ding, JP |
刊名 | PLOS ONE
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出版日期 | 2012 |
卷号 | 7期号:9页码:e44828-e44828 |
通讯作者 | Ding, JP (reprint author), Chinese Acad Sci, Shanghai Inst Biol Sci, Inst Biochem & Cell Biol, State Key Lab Mol Biol, Shanghai, Peoples R China.,jpding@sibs.ac.cn |
英文摘要 | Human calcium/calmodulin-dependent protein kinase I (CaMKI) plays pivotal roles in the nervous system. The activity of human CaMKI is regulated by a regulatory region including an autoinhibitory segment and a CaM-binding segment. We report here four structures of three CaMKI alpha truncates in apo form and in complexes with ATP. In an apo, autoinhibited structure, the activation segment adopts a unique helical conformation which together with the autoinhibitory segment constrains helices alpha C and alpha D in inactive conformations, sequesters Thr177 from being phosphorylated, and occludes the substrate-binding site. In an ATP-bound, inactive structure, the activation segment is largely disordered and the CaM-binding segment protrudes out ready for CaM binding. In an ATP-bound, active structure, the regulatory region is dissociated from the catalytic core and the catalytic site assumes an active conformation. Detailed structural analyses reveal the interplay of the regulatory region, the activation segment, and the nucleotide-binding site in the regulation of CaMKI. |
学科主题 | Science & Technology - Other Topics |
类目[WOS] | Multidisciplinary Sciences |
关键词[WOS] | DEPENDENT PROTEIN-KINASE ; GROWTH-FACTOR RECEPTOR ; CALMODULIN ; COMPLEX ; ACTIVATION ; PHOSPHORYLATION ; TRANSCRIPTION ; POTENTIATION ; BINDING ; CYCLIN |
收录类别 | SCI |
语种 | 英语 |
WOS记录号 | WOS:000309388900012 |
版本 | 出版稿 |
源URL | [http://202.127.25.143/handle/331003/637] ![]() |
专题 | 上海生化细胞研究所_上海生科院生化细胞研究所 |
推荐引用方式 GB/T 7714 | Zha, MW,Zhong, C,Ou, Y,et al. Crystal Structures of Human CaMKI alpha Reveal Insights into the Regulation Mechanism of CaMKI[J]. PLOS ONE,2012,7(9):e44828-e44828. |
APA | Zha, MW,Zhong, C,Ou, Y,Han, L,Wang, JC,&Ding, JP.(2012).Crystal Structures of Human CaMKI alpha Reveal Insights into the Regulation Mechanism of CaMKI.PLOS ONE,7(9),e44828-e44828. |
MLA | Zha, MW,et al."Crystal Structures of Human CaMKI alpha Reveal Insights into the Regulation Mechanism of CaMKI".PLOS ONE 7.9(2012):e44828-e44828. |
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