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h3 class=""
h3"">Summary
h3>Evolution of minimal DNA tumor virus' genomes
has selected for small viral oncoproteins t
hat
hijack critical cellular protein interaction networks. T
he structural basis for t
he multiple and dominant functions of adenovirus oncoproteins
has remained elusive. E4-ORF3 forms a nuclear polymer and simultaneously inactivates p53, PML, TRIM24, and MRE11/RAD50/NBS1 (MRN) tumor suppressors. We identify oligomerization mutants and solve t
he crystal structure of E4-ORF3. E4-ORF3 forms a dimer wit
h?a central ¦Â core, and its structure is unrelated to known polymers or oncogenes. E4-ORF3 dimer units coassemble t
hroug
h reciprocal and nonreciprocal exc
hanges of t
heir C-terminal tails. T
his results in linear and branc
hed oligomer c
hains t
hat furt
her assemble in variable arrangements to form a polymer network t
hat partitions t
he nuclear volume. E4-ORF3 assembly creates avidity-driven interactions wit
h PML and an emergent MRN binding interface. T
his reveals an elegant structural solution w
hereby a small protein forms a multivalent matrix t
hat traps disparate tumor suppressors.<
h4 class=""
h4"">PaperFlick
h4>
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