Taxonomic distribution of proteins containing CDT1 domains

The tree below includes only several representative species and genera. The complete taxonomic breakdown of all proteins containing CDT1 domains can be accessed here. Click the counts or percentage values to display the corresponding proteins.

Structural basis for inhibition of the replication licensing factor Cdt1by geminin.

Lee C, Hong B, Choi JM, Kim Y, Watanabe S, Ishimi Y, Enomoto T, Tada S, Kim Y, Cho Y
Nature. 2004; 430: 913-7

To maintain chromosome stability in eukaryotic cells, replication originsmust be licensed by loading mini-chromosome maintenance (MCM2-7) complexesonce and only once per cell cycle. This licensing control is achievedthrough the activities of geminin and cyclin-dependent kinases. Gemininbinds tightly to Cdt1, an essential component of the replication licensingsystem, and prevents the inappropriate reinitiation of replication on analready fired origin. The inhibitory effect of geminin is thought toprevent the interaction between Cdt1 and the MCM helicase. Here wedescribe the crystal structure of the mouse geminin-Cdt1 complex usingtGeminin (residues 79-157, truncated geminin) and tCdt1 (residues 172-368,truncated Cdt1). The amino-terminal region of a coiled-coil dimer oftGeminin interacts with both N-terminal and carboxy-terminal parts oftCdt1. The primary interface relies on the steric complementarity betweenthe tGeminin dimer and the hydrophobic face of the two short N-terminalhelices of tCdt1 and, in particular, Pro 181, Ala 182, Tyr 183, Phe 186and Leu 189. The crystal structure, in conjunction with our biochemicaldata, indicates that the N-terminal region of tGeminin might be requiredto anchor tCdt1, and the C-terminal region of tGeminin prevents access ofthe MCM complex to tCdt1 through steric hindrance.