| Автор | Toyoshima, Chikashi |
| Автор | Inesi, Giuseppe |
| Дата выпуска | 2004 |
| dc.description | ▪ Abstract The structures of the Ca<sup>2+</sup>-ATPase (SERCA1a) have been determined for five different states by X-ray crystallography. Detailed comparison of the structures in the Ca<sup>2+</sup> bound form and unbound (but thapsigargin bound) form reveals that very large rearrangements of the transmembrane helices take place accompanying Ca<sup>2+</sup> dissociation and binding and that they are mechanically linked with equally large movements of the cytoplasmic domains. The meanings of the rearrangements of the transmembrane helices and those of the cytoplasmic domains as well as the mechanistic roles of phosphorylation are now becoming clear. Furthermore, the roles of critical amino acid residues identified by extensive mutagenesis studies are becoming evident in terms of atomic structure. |
| Формат | application.pdf |
| Издатель | Annual Reviews |
| Копирайт | Annual Reviews |
| Название | STRUCTURAL BASIS OF ION PUMPING BY CA<sup>2+</sup>-ATPASE OF THE SARCOPLASMIC RETICULUM |
| DOI | 10.1146/annurev.biochem.73.011303.073700 |
| Print ISSN | 0066-4154 |
| Журнал | Annual Review of Biochemistry |
| Том | 73 |
| Первая страница | 269 |
| Последняя страница | 292 |
| Аффилиация | Toyoshima, Chikashi; Institute of Molecular and Cellular Biosciences, The University of Tokyo, Tokyo 113-0032, Japan; email: ct@iam.u-tokyo.ac.jp |
