Crystal Structures of N-terminal Domain of Human Hsp90 With ATP Analogues Reveal The Functional Regulation of Hsp90
文献类型：期刊论文
| 作者 | Li, J（李健） ; Sun, LH（孙丽华） ; Xu, CY（徐春艳） ; Yu, F（郁峰） ; Zhou, H（周欢） ; Tang, L（唐琳） ; He, JH（何建华） |
| 刊名 | PROGRESS IN BIOCHEMISTRY AND BIOPHYSICS
 |
| 出版日期 | 2012 |
| 卷号 | 39期号:10 |
| ISSN号 | 1000-3282 |
| 英文摘要 | Heat shock protein 90 (Hsp90) is essential for folding, maturation and stabilization of many important proteins, which are involved in cell cycle regulation, signal transduction, and cell growth regulation. The highly conserved N-terminal domain contains an ATP binding cleft and thus is responsible for the catalytic activity of Hsp90. In order to further study the function and structure of Hsp90, the N-terminal of the human Hsp90 was cocrystallized with AMPPNP and ATP gamma S. The cocrystallization experiments were carried out at 277K using the hanging drop vapor-diffusion method, X-ray diffraction data were collected on beamline 17U at the SSRF and the structures were solved by molecular replacement. The densities of the two nucleotides were captured and the interactions between Hsp90(N) and nucleotides were clearly described. We confirmed that the gamma-phosphate of ATP gamma S was not hydrolyzed by Hsp90(N). The position of S 1 and ATP lid in human Hsp90(N)-AMPPNP differs significantly from that of the structure of yeast Hsp90-AMPPNP. By analyzing the structure of human Hsp90(N)-AMPPNP, we found that the interactions of E18-K100 and N40-D127 block the moving of Si and ATP lid, and then prevent the dimerization of Hsp90(N). This reflects the complexity and coordination of Hsp90 on the regulation of the function. |
| 语种 | 英语 |
| WOS记录号 | WOS:000310118300009 |
| 公开日期 | 2013-09-11 |
| 源URL | [http://ir.sinap.ac.cn/handle/331007/13113]  |
| 专题 | 上海应用物理研究所_中科院上海应用物理研究所2011-2017年 |
| 推荐引用方式 GB/T 7714 | Li, J,Sun, LH,Xu, CY,et al. Crystal Structures of N-terminal Domain of Human Hsp90 With ATP Analogues Reveal The Functional Regulation of Hsp90[J]. PROGRESS IN BIOCHEMISTRY AND BIOPHYSICS,2012,39(10). |
| APA | Li, J.,Sun, LH.,Xu, CY.,Yu, F.,Zhou, H.,...&He, JH.(2012).Crystal Structures of N-terminal Domain of Human Hsp90 With ATP Analogues Reveal The Functional Regulation of Hsp90.PROGRESS IN BIOCHEMISTRY AND BIOPHYSICS,39(10). |
| MLA | Li, J,et al."Crystal Structures of N-terminal Domain of Human Hsp90 With ATP Analogues Reveal The Functional Regulation of Hsp90".PROGRESS IN BIOCHEMISTRY AND BIOPHYSICS 39.10(2012). |
入库方式： OAI收割
来源：上海应用物理研究所
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