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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

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Leitner, D. et al.

Leitner, Wahl, Labudde, Krause, Diehl, Schmieder, Pires, Fossi, Wiedemann, Leidert, Oschkinat,

The solution structure of an N-terminally truncated version of the yeast CDC24p PB1 domain shows a different beta-sheet topology.

Phox and Bem1 (PB1) domains mediate protein-protein interactions via the formation of homo- or hetero-dimers. The C-terminal PB1 domain of yeast cell division cycle 24 (CDC24p), a guanine-nucleotide exchange factor involved in cell polarity establishment, is known to interact with the PB1 domain occurring in bud emergence MSB1 interacting 1 (BEM1p) during the regulation of the yeast budding process via its OPR/PC/AID (OPCA) motif. Here, we present the structure of an N-terminally truncated version of the Sc CDC24p PB1 domain. It shows a different topology of the beta-sheet than the long form. However, the C-terminal part of the structure shows the conserved PB1 domain features including the OPCA motif with a slight rearrangement of helix alpha1. Residues which are important for the heterodimerization with BEM1p are structurally preserved.[1]

References

The solution structure of an N-terminally truncated version of the yeast CDC24p PB1 domain shows a different beta-sheet topology. Leitner, D., Wahl, M., Labudde, D., Krause, G., Diehl, A., Schmieder, P., Pires, J.R., Fossi, M., Wiedemann, U., Leidert, M., Oschkinat, H. FEBS Lett. (2005) [Pubmed]

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