Crystal Structures of Tcl1 Family Oncoproteins and Their Conserved Surface Features

• Main Authors: John M. Petock, Ivan Y. Torshin, Yuan-Fang Wang, Garrett C. Du Bois, Carlo M. Croce, Robert W. Harrison, Irene T. Weber
• Format: Article
• Language: English
• Published: Hindawi Limited 2002-01-01
• Series: The Scientific World Journal
• Online Access: http://dx.doi.org/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 ~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).