Crystal structure of the N-terminal domain of human Timeless and its interaction with Tipin
Nucleic Acids Research
Oxford University Press
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Holzer, S., Degliesposti, G., Kilkenny, M., Maslen, S., Matak-Vinkovíc, D., Skehel, M., & Pellegrini, L. (2017). Crystal structure of the N-terminal domain of human Timeless and its interaction with Tipin. Nucleic Acids Research, (gkx139)https://doi.org/10.1093/nar/gkx139
Human Timeless is involved in replication fork stabilization, S-phase checkpoint activation and establishment of sister chromatid cohesion. In the cell, Timeless forms a constitutive heterodimeric complex with Tipin. Here we present the 1.85 Å crystal structure of a large N-terminal segment of human Timeless, spanning amino acids 1-463, and we show that this region of human Timeless harbours a partial binding site for Tipin. Furthermore, we identify minimal regions of the two proteins that are required for the formation of a stable Timeless-Tipin complex and provide evidence that the Timeless-Tipin interaction is based on a composite binding interface comprising different domains of Timeless.
Wellcome Trust Investigator Award [104641/Z/14/Z to L.P.]; Boehringer-Ingelheim Fonds PhD Fellowship; Janggen-Pöhn-Stiftung Awards; Swiss National Science Foundation (to S.H.). Funding for open access charge: Wellcome Trust.
WELLCOME TRUST (104641/Z/14/Z)
External DOI: https://doi.org/10.1093/nar/gkx139
This record's URL: https://www.repository.cam.ac.uk/handle/1810/263590
Attribution 4.0 International, Attribution 4.0 International, Attribution 4.0 International, Attribution 4.0 International, Attribution 4.0 International