SIOTSFROAK · Structural Investigations On The Structure-Function Relationships of Aurora Kinases
6РП — Действия „Мария Кюри“
- Период
- 2005-11-01 → 2007-10-31
- Финансиране от ЕС
- 149 722 €
- Участници
- 1
- Схема
- IIF
Линиите свързват координатора с партньорите.
Накратко на български
Протеините Aurora кинази, които регулират деленето на клетките, се изследват чрез рентгенова кристалография при хора, плодови мухи и червеи. Това помага да се разбере молекулният механизъм, по който тези ензими се активират и контролират процесите в организма.
Кратко обяснение, генерирано от езиков модел по текста на CORDIS. Оригиналът е по-долу.
Цел на проекта
Aurora protein kinases belong to the family of serine/threonine protein kinases. They are evolutionarily conserved enzymes that regulate different aspects of cell division. In vertebrates, there exists three Aurora kinases namely, Aurora A, Aurora B and Aurora C. In contrast, the C. elegans and D. melanogaster genomes encode only for two Aurora orthologues and the S. cerevisiae genome for a single one. Aurora kinases differ in length and sequence of the amino terminal domain (non-catalytic domain), but show considerable sequence similarity in the carboxy-terminal catalytic domain. Interestingly, even in the presence of high sequence similarity the three Aurora kinases are localized in distinct locations and perform different functions. Aurora A is shown to play a major role in centrosome separation, centrosome maturation and in the stabilization of mitotic spindle assembly, while the Aurora B is important in the regulation of kinetochore-microtuble interactions. The function of Aurora A is conserved in human, Xenopus, Drosophila and C. elegans. Recent studies that include crystallographic structural studies from the host laboratory showed the role of TPX2, an activator of human Aurora A in molecular recognition and regulation. Although the function of Aurora A is conserved in human, Xenopus, Drosophila and C. elegans, there is no apparent homologue of TPX2 in their respective genomes. In a similar note, the Auroras A and B share very high sequence identity but their respective activators TPX2 and INCENP do not show any reasonable sequence similarity. The proposed project aims to understand the molecular mechanism involved in the activation and regulation of Aurora A from C. elegans and Drosophila and of human Aurora B mainly using X-ray crystallographic methods. Since, Aurora proteins are oncogens, the structural information derived from this study would help in designing specific inhibitors to block their activation.
Оригинален текст от CORDIS (на английски).
Участници
- EUROPEAN MOLECULAR BIOLOGY LABORATORY · HEIDELBERGКоординаторГермания
Връзки
Данни: CORDIS, © Европейски съюз