Crystal structure of human multiple copies in T‐cell lymphoma‐1 oncoprotein

Overexpression of multiple copies in T‐cell lymphoma‐1 (MCT‐1) oncogene accompanies malignant phenotypic changes in human lymphoma cells. Specific disruption of MCT‐1 results in reduced tumorigenesis, suggesting a potential for MCT‐1‐targeted therapeutic strategy. MCT‐1 is known as a cap‐binding protein and has a putative RNA‐binding motif, the PUA‐domain, at its C‐terminus. We determined the crystal structure of apo MCT‐1 at 1.7 Å resolution using the surface entropy reduction method. Notwithstanding limited sequence identity to its homologs, the C‐terminus of MCT‐1 adopted a typical PUA‐domain fold that includes secondary structural elements essential for RNA recognition. The surface of the N‐terminal domain contained positively charged patches that are predicted to contribute to RNA‐binding. Proteins 2013. © 2012 Wiley Periodicals, Inc.