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Amino acids 1-107 of the SV40 T antigen constitute a functionally important and complex region. Cellular proteins, Hsc70, Bub-1, Cul-7, and Rb, each of which is involved in cell growth control or genomic stability, bind within this portion of the T antigen. Mutational analysis has mapped the J domain/Hsc70, Bub-1, and the Rb binding motifs. Two regions of the T antigen have been implicated in Cul-7 binding. Mutation of F98A diminished Cul-7 binding, and deletion of amino acids 68-83 abolished it. The authors suggest, based on T-antigen structure, that F98 is inaccessible and that the F98A change altered the configuration of the upstream region, preventing Cul-7 binding. Our objective was to determine, by using monoclonal T-antigen antibodies, whether F98 is accessible and whether F98A substitution globally distorted the T-common region.

SV40 T-Antigen Amino Acid Changes that Disrupt Cul-7 or Bub-1 Binding Do Not Globally Distort the T-Common Region