Tcl1家族癌蛋白的晶体结构及其保守的表面特征。
Crystal structures of Tcl1 family oncoproteins and their conserved surface features.
作者信息
Petock John M, Torshin Ivan Y, Wang Yuan-Fang, Du Bois Garrett C, Croce Carlo M, Harrison Robert W, Weber Irene T
机构信息
Department of Biology, Georgia State University, Atlanta, GA, USA.
出版信息
ScientificWorldJournal. 2002 Jul 4;2:1876-84. doi: 10.1100/tsw.2002.826.
Members of the TCL1 family of oncogenes are abnormally expressed in mature T-cell leukemias and B-cell lymphomas. The proteins are involved in the coactivation of protein kinase B (Akt/PKB), a key intracellular kinase. The sequences and crystal structures of three Tcl1 proteins were analyzed in order to understand their interactions with Akt/PKB and the implications for lymphocyte malignancies. Tcl1 proteins are approximately 15 kD and share 25-80% amino acid sequence identity. The tertiary structures of mouse Tcl1, human Tcl1, and Mtcp1 are very similar. Analysis of the structures revealed conserved semi-planar surfaces that have characteristics of surfaces involved in protein-protein interactions. The Tcl1 proteins show differences in surface charge distribution and oligomeric state suggesting that they do not interact in the same way with Akt/PKB and other cellular protein(s).
原癌基因TCL1家族成员在成熟T细胞白血病和B细胞淋巴瘤中异常表达。这些蛋白质参与蛋白激酶B（Akt/PKB，一种关键的细胞内激酶）的共激活。为了了解三种Tcl1蛋白与Akt/PKB的相互作用以及对淋巴细胞恶性肿瘤的影响，对它们的序列和晶体结构进行了分析。Tcl1蛋白约为15 kD，氨基酸序列同一性为25 - 80%。小鼠Tcl1、人Tcl1和Mtcp1的三级结构非常相似。结构分析揭示了保守的半平面表面，这些表面具有参与蛋白质 - 蛋白质相互作用的表面特征。Tcl1蛋白在表面电荷分布和寡聚状态上存在差异，这表明它们与Akt/PKB和其他细胞蛋白的相互作用方式不同。
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