Crystal structures of Tcl1 family oncoproteins and their conserved surface features.
Crystal structures of Tcl1 family oncoproteins and their conserved surface features.
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DOI：
10.1100/tsw.2002.826
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发表时间：
2002-07-04
影响因子：
--
通讯作者：
Weber IT
中科院分区：
文献类型：
--
作者：
Petock JM;Torshin IY;Wang YF;Du Bois GC;Croce CM;Harrison RW;Weber IT
癌基因的TCL 1家族的成员在成熟的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/PK B）的共活化，蛋白激酶B是一种关键的细胞内激酶。分析了三种Tcl 1蛋白的序列和晶体结构，以了解它们与Akt/PKB的相互作用及其对淋巴细胞恶性肿瘤的影响。Tcl 1蛋白约为15 kD，共有25-80%的氨基酸序列同一性。小鼠Tcl 1、人Tcl 1和Mtcp 1的三级结构非常相似。结构分析表明，保守的半平面表面，具有参与蛋白质-蛋白质相互作用的表面特征。Tcl 1蛋白在表面电荷分布和寡聚状态方面显示出差异，这表明它们不以相同的方式与Akt/PKB和其他细胞蛋白相互作用。
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 ~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).