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TitleStructure of the Cdt1 C-terminal domain: Conservation of the winged helix fold in replication licensing factors
Journal, issue, pagesProtein Sci., Vol. 18, Page 2252-2264, Year 2009
Publish dateJul 6, 2009 (structure data deposition date)
AuthorsKhayrutdinov, B.I. / Bae, W.J. / Yun, Y.M. / Lee, J.H. / Tsuyama, T. / Kim, J.J. / Hwang, E. / Ryu, K.-S. / Cheong, H.-K. / Cheong, C. ...Khayrutdinov, B.I. / Bae, W.J. / Yun, Y.M. / Lee, J.H. / Tsuyama, T. / Kim, J.J. / Hwang, E. / Ryu, K.-S. / Cheong, H.-K. / Cheong, C. / Ko, J.-S. / Enomoto, T. / Karplus, P.A. / Guntert, P. / Tada, S. / Jeon, Y.H. / Cho, Y.
External linksProtein Sci. / PubMed:19722278
MethodsNMR (solution) / X-ray diffraction
Resolution1.889 Å
Structure data

PDB-2klo:
Structure of the Cdt1 C-terminal domain
Method: SOLUTION NMR

PDB-3a4c:
Crystal structure of cdt1 C terminal domain
Method: X-RAY DIFFRACTION / Resolution: 1.889 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • mus musculus (house mouse)
KeywordsCELL CYCLE / mouse Cdt1 / replication licensing factor / winged helix fold / mcm binding / DNA replication / DNA-binding / Nucleus / Phosphoprotein / Proto-oncogene / Ubl conjugation / Replication / alpha-beta structure

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