Investigating the Structural Mechanisms and Features of KCTD9

真核细胞利用泛素蛋白体系统降解蛋白质并调节其活性。E3连接酶是一类蛋白质，其作为该过程的关键组分。最近，这些蛋白质在几个医学和生物学研究领域受到关注。主要项目将寻求通过X射线晶体学确定KCTD 9的结构，并通过亲和蛋白质组学鉴定底物蛋白。然后将表征支配E3连接酶与这些底物之间相互作用的结构特征。还将探讨泛素化活性，细胞作用以及KCTD 9对自然杀伤细胞发育的影响。第二个项目的目标是开发一种新的化学探针，用于不同的cullin RING连接酶FBXO 31。FBXO 31的结构数据将有助于该探头的开发和优化。BBSRC将优先考虑解决生物学或正常人体生理学中重要基础问题的基础科学，这可以促进许多领域的知识和创新。

Eukaryotic cells use the ubiquitin proteosome system to degrade proteins and regulate their activity. E3 ligases are a class of proteins which act as a key component for this process. Recently, these proteins have received interest in several medicinal and biological research fields. The primary project will seek to determine the structure of KCTD9 by x-ray crystallography and identify substrate proteins with affinity proteomics. The structural features which govern the interactions between the E3 ligase and these substrates will then be characterized. The ubiquitination activity, the cellular role, and the implication KCTD9 has on natural killer cell development will also be explored. A secondary project will aim to develop a novel chemical probe for a different cullin RING ligase, FBXO31. The structural data of FBXO31 will aid the development and optimization of this probe. The probe will then be validated for in vitro study of FBXO31 and additional functions can be examined.BBSRC will give priority to fundamental science which addresses important underpinning questions in biology or normal human physiology, which can advance knowledge and innovation across many sectors.