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Resolution: standard / high Figure 1.
Alignment of key functional domains of MCPyV, JC, and SV40 large T antigens. At the
top is a cartoon of the protein structure of the predicted MCPyV large T antigen,
based on its homology to the well-characterized SV40 large T antigen (modified from
[17]). Underneath are expanded alignments for the Hsc70-binding motif and the pRb-binding
motif, comparing the putative MCPyV large T antigen with the JC and SV40 large T antigens.
Importantly, as indicated by the bold underlines below the zoom-ins, both the HPDK
Hsc70-binding motif and the LxCxEx Rb-binding motifs are preserved in the predicted
MCPyV large T antigen. Noted on the cartoon are the locations of the premature stop
(MCV350) and frameshift (MCV339) mutations of the two known MCPyV genomes [11]. These
predicted truncated proteins potentially preserve some of the cell-cycle progression
activities of the amino terminus of large T but prevent cell-lethal genomic instability
related to the replicative functions of the carboxyl terminus.
Garneski et al. Genome Biology 2008 9:228 doi:10.1186/gb-2008-9-6-228 |