1UII

Crystal structure of Geminin coiled-coil domain

Summary for 1UII

• Entry DOI: 10.2210/pdb1uii/pdb
• Descriptor: Geminin (2 entities in total)
• Functional Keywords: geminin, human, dna replication, cell cycle
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 2
• Total formula weight: 19529.89

Authors

Yuan, P.,Swaminathan, K.,Robinson, H. (deposition date: 2003-07-16, release date: 2004-07-16, Last modification date: 2023-12-27)

Primary citation

Saxena, S.,Yuan, P.,Dhar, S.K.,Senga, T.,Takeda, D.,Robinson, H.,Kornbluth, S.,Swaminathan, K.,Dutta, A.
A dimerized coiled-coil domain and an adjoining part of geminin interact with two sites on Cdt1 for replication inhibition
Mol.Cell, 15:245-258, 2004

PubMed Abstract: Geminin is a cellular protein that associates with Cdt1 and inhibits Mcm2-7 loading during S phase. It prevents multiple cycles of replication per cell cycle and prevents episome replication. It also directly inhibits the HoxA11 transcription factor. Here we report that geminin forms a parallel coiled-coil homodimer with atypical residues in the dimer interface. Point mutations that disrupt the dimerization abolish interaction with Cdt1 and inhibition of replication. An array of glutamic acid residues on the coiled-coil domain surface interacts with positive charges in the middle of Cdt1. An adjoining region interacts independently with the N-terminal 100 residues of Cdt1. Both interactions are essential for replication inhibition. The negative residues on the coiled-coil domain and a different part of geminin are also required for interaction with HoxA11. Therefore a rigid cylinder with negative surface charges is a critical component of a bipartite interaction interface between geminin and its cellular targets.

PubMed: 15260975
DOI: 10.1016/j.molcel.2004.06.045

Experimental method

X-RAY DIFFRACTION (2 Å)