Crystal Structures of Tcl1 Family Oncoproteins and Their Conserved Surface Features. (2002)

• Record Type: Journal Article
• Authors: Petock, John M.; Torshin, Ivan Y.; Wang, Yuan-Fang; Du Bois, Garrett C.; Croce, Carlo M.; Harrison, Robert W.; Weber, Irene T.
• Is Part Of: TheScientificWorldjournal. Volume 2(2002)
• Page Start: 1876
• Page End: 1884
• Publication Date: 2002
• Subjects: leukemia -- oncoprotein -- Tcl1 -- Akt/protein kinase B -- X-ray crystallography; Science -- Periodicals; Technology -- Periodicals; Medicine -- Periodicals; 505
• DOI: 10.1100/tsw.2002.826
• Languages: English
• ISSNs: 2356-6140

Abstract

Abstract : 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).