| Автор | Arnaout, M.A. |
| Автор | Mahalingam, B. |
| Автор | Xiong, J.-P. |
| Дата выпуска | 2005 |
| dc.description | Abstract αβ heterodimeric integrins mediate dynamic adhesive cell-cell and cell-extracellular matrix (ECM) interactions in metazoa that are critical in growth and development, hemostasis, and host defense. A central feature of these receptors is their capacity to change rapidly and reversibly their adhesive functions by modulating their ligand-binding affinity. This is normally achieved through interactions of the short cytoplasmic integrin tails with intracellular proteins, which trigger restructuring of the ligand-binding site through long-range conformational changes in the ectodomain. Ligand binding in turn elicits conformational changes that are transmitted back to the cell to regulate diverse responses. The publication of the integrin αVβ3 crystal structure has provided the context for interpreting decades-old biochemical studies. Newer NMR, crystallographic, and EM data, reviewed here, are providing a better picture of the dynamic integrin structure and the allosteric changes that guide its diverse functions. |
| Формат | application.pdf |
| Издатель | Annual Reviews |
| Копирайт | Annual Reviews |
| Название | INTEGRIN STRUCTURE, ALLOSTERY, AND BIDIRECTIONAL SIGNALING |
| DOI | 10.1146/annurev.cellbio.21.090704.151217 |
| Print ISSN | 1081-0706 |
| Журнал | Annual Review of Cell and Developmental Biology |
| Том | 21 |
| Первая страница | 381 |
| Последняя страница | 410 |
| Аффилиация | Arnaout, M.A.; Structural Biology Program, Leukocyte Biology and Inflammation Program, Nephrology Division, Department of Medicine, Massachusetts General Hospital and Harvard Medical School, Charlestown, Massachussetts 02129; email: arnaout@receptor.mgh.harvard.edu , bmahalingam@partners.org , xiong@helix.mgh.harvard.edu |
