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Volume 2, Pages 1876-1884
Mini-Review Article

Crystal Structures of Tcl1 Family Oncoproteins and Their Conserved Surface Features

1Department of Biology, Georgia State University, Atlanta, GA, USA
2Department of Computer Science, Georgia State University, Atlanta, GA, USA
3Department of Microbiology and Immunology, Kimmel Cancer Center, Thomas Jefferson University, Philadelphia, PA, USA

Received 12 February 2001; Revised 9 May 2002; Accepted 13 May 2002

Copyright © 2002 John M. Petock et al.


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).