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This research aims to elucidate the NMR structure of the N-terminal J domain of murine polyomavirus T antigens.

NMR Structure of the N-terminal J Domain of Murine Polyomavirus T Antigens

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This research aims to elucidate the NMR structure of the N-terminal J domain of murine polyomavirus T antigens.
Determined the NMR structure of the N-terminal DnaJ-like domain of murine polyomavirus T antigens.
Measured high precision with root mean square deviations of 0.38 A for backbone atoms and 0.94 A for all heavy atoms.
Tested functional implications in Escherichia coli using chimeras with mutations.
PyJ exhibits a three-helix fold similar to other J domains, with significant differences in helix lengths.
Glutamine residues on helix II surface replace positive charges typical for J domains but retain functionality.
Mutations in T antigen cluster in areas crucial for cellular transformation, affecting interactions with PP2A.

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NMR determination of the PyJ structure reveals key features and functional implications for T antigens.

Berjanskii et al. (2000) studied this question.

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