Journal
NUCLEIC ACIDS RESEARCH
Volume 45, Issue 9, Pages 5555-5563Publisher
OXFORD UNIV PRESS
DOI: 10.1093/nar/gkx139
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Funding
- Wellcome Trust Investigator Award [104641/Z/14/Z]
- Boehringer-Ingelheim Fonds PhD Fellowship
- Janggen-Pohn-Stiftung Awards
- Swiss National Science Foundation
- Wellcome Trust
- Wellcome Trust [104641/Z/14/Z] Funding Source: Wellcome Trust
- MRC [MC_U105178788] Funding Source: UKRI
- Medical Research Council [MC_U105178788] Funding Source: researchfish
- Wellcome Trust [104641/Z/14/Z] Funding Source: researchfish
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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 angstrom 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.
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