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Crystallization and preliminary X-ray diffraction studies of FHA domains of Dun1 and Rad53 protein kinases

Journal Article


Abstract


  • Forkhead-associated (FHA) domains are modular protein-protein interaction domains of ∼130 amino acids present in numerous signalling proteins. FHA-domain-dependent protein interactions are regulated by phosphorylation of target proteins and FHA domains may be multifunctional phosphopeptide-recognition modules. FHA domains of the budding yeast cell-cycle checkpoint protein kinases Dun1p and Rad53p have been crystallized. Crystals of the Dun1-FHA domain exhibit the symmetry of the space group P6122 or P6522, with unit-cell parameters a = b = 127.3, c = 386.3 Å; diffraction data have been collected to 3.1 Å resolution on a synchrotron source. Crystals of the N-terminal FHA domain (FHA1) of Rad53p diffract to 4.0 Å resolution on a laboratory X-ray source and have Laue-group symmetry 4/mmm, with unit-cell parameters a = b = 61.7, c = 104.3 Å.

UOW Authors


  •   Blanchard, Helen (external author)

Publication Date


  • 2001

Citation


  • Blanchard, H., Fontes, M. R. M., Hammet, A., Pike, B. L., Teh, T., Gleichmann, T., . . . Heierhorst, J. (2001). Crystallization and preliminary X-ray diffraction studies of FHA domains of Dun1 and Rad53 protein kinases. Acta Crystallographica Section D: Biological Crystallography, 57(3), 459-461. doi:10.1107/S0907444901002116

Scopus Eid


  • 2-s2.0-0035093089

Start Page


  • 459

End Page


  • 461

Volume


  • 57

Issue


  • 3

Abstract


  • Forkhead-associated (FHA) domains are modular protein-protein interaction domains of ∼130 amino acids present in numerous signalling proteins. FHA-domain-dependent protein interactions are regulated by phosphorylation of target proteins and FHA domains may be multifunctional phosphopeptide-recognition modules. FHA domains of the budding yeast cell-cycle checkpoint protein kinases Dun1p and Rad53p have been crystallized. Crystals of the Dun1-FHA domain exhibit the symmetry of the space group P6122 or P6522, with unit-cell parameters a = b = 127.3, c = 386.3 Å; diffraction data have been collected to 3.1 Å resolution on a synchrotron source. Crystals of the N-terminal FHA domain (FHA1) of Rad53p diffract to 4.0 Å resolution on a laboratory X-ray source and have Laue-group symmetry 4/mmm, with unit-cell parameters a = b = 61.7, c = 104.3 Å.

UOW Authors


  •   Blanchard, Helen (external author)

Publication Date


  • 2001

Citation


  • Blanchard, H., Fontes, M. R. M., Hammet, A., Pike, B. L., Teh, T., Gleichmann, T., . . . Heierhorst, J. (2001). Crystallization and preliminary X-ray diffraction studies of FHA domains of Dun1 and Rad53 protein kinases. Acta Crystallographica Section D: Biological Crystallography, 57(3), 459-461. doi:10.1107/S0907444901002116

Scopus Eid


  • 2-s2.0-0035093089

Start Page


  • 459

End Page


  • 461

Volume


  • 57

Issue


  • 3