Yu Grace W, Allen Mark D, Andreeva Antonina, Fersht Alan R, Bycroft Mark
Centre for Protein Engineering, Medical Research Council, Hills Road, CB2 2QH, Cambridge, United Kingdom.
Protein Sci. 2006 Feb;15(2):384-9. doi: 10.1110/ps.051927306. Epub 2005 Dec 29.
HDM2 is a ubiquitin E3 ligase that is a key negative regulator of the tumor suppressor p53. Here, we report the determination of the solution structure of the C4 zinc finger domain of HDM2 using multidimensional NMR. The HDM2 C4 zinc finger domain has a fold consisting of a 3(10) helix followed by four beta-strands, which shares significant structural similarity to the zinc ribbon protein family. Family based sequence analysis identified two putative binding sites, one of which resembles an RNA binding motif.
HDM2是一种泛素E3连接酶,是肿瘤抑制因子p53的关键负调控因子。在此,我们报告了使用多维核磁共振确定HDM2的C4锌指结构域的溶液结构。HDM2的C4锌指结构域具有由一个3(10)螺旋和随后的四条β链组成的折叠结构,与锌带蛋白家族具有显著的结构相似性。基于家族的序列分析确定了两个假定的结合位点,其中一个类似于RNA结合基序。