人p73α C末端SAM结构域的结晶及初步晶体学研究
Crystallization and preliminary crystallographic studies of a SAM domain at the C-terminus of human p73alpha.
作者信息
Wang W K, Proctor M R, Buckle A M, Bycroft M, Chen Y W
机构信息
Cambridge University Chemical Laboratory and Centre for Protein Engineering, MRC Centre, Cambridge, England.
出版信息
Acta Crystallogr D Biol Crystallogr. 2000 Jun;56(Pt 6):769-71. doi: 10.1107/s0907444900005059.
p73 is a recently discovered homologue of the tumour suppressor p53 and contains all three functional domains of p53. The alpha-splice variant of p73 (p73alpha) contains an additional structural domain near its C--terminus that has sequence homology with the sterile alpha-motif (SAM) domain. This domain is considered to be responsible for mediating protein-protein interactions. Pyramidal crystals of human p73alpha SAM domain were obtained by the hanging-drop vapour-diffusion method with ammonium dihydrogen orthophosphate as the precipitant. The crystals diffract to 2.54 A resolution and belong to the tetragonal space group P4(1)2(1)2, with unit-cell parameters a = b = 32.02, c = 133.84 A. The structure was solved by molecular replacement using the NMR structure of the same protein as the search model.
p73是最近发现的肿瘤抑制因子p53的同源物，包含p53的所有三个功能结构域。p73的α剪接变体（p73α）在其C末端附近包含一个额外的结构域，该结构域与无活性α基序（SAM）结构域具有序列同源性。该结构域被认为负责介导蛋白质-蛋白质相互作用。通过以磷酸二氢铵为沉淀剂的悬滴气相扩散法获得了人p73α SAM结构域的棱柱状晶体。这些晶体的衍射分辨率为2.54 Å，属于四方晶系空间群P4(1)2(1)2，晶胞参数a = b = 32.02，c = 133.84 Å。通过使用相同蛋白质的NMR结构作为搜索模型的分子置换法解析了该结构。
Zotero 插件