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2KLQ

The solution structure of CBD of human MCM6

Summary for 2KLQ
Entry DOI10.2210/pdb2klq/pdb
NMR InformationBMRB: 16396
DescriptorDNA replication licensing factor MCM6 (1 entity in total)
Functional Keywordsdna replication, pre-rc, mcm6, cdt1, cbd structure, atp-binding, cell cycle, dna-binding, nucleotide-binding, nucleus, phosphoprotein, polymorphism, transcription, transcription regulation, replication
Biological sourceHomo sapiens (human)
Cellular locationNucleus: Q14566
Total number of polymer chains1
Total formula weight13303.88
Authors
Liu, C. (deposition date: 2009-07-08, release date: 2010-03-02, Last modification date: 2024-05-29)
Primary citationWei, Z.,Liu, C.,Wu, X.,Xu, N.,Zhou, B.,Liang, C.,Zhu, G.
Characterization and structure determination of the Cdt1 binding domain of human minichromosome maintenance (Mcm) 6
J.Biol.Chem., 285:12469-12473, 2010
Cited by
PubMed Abstract: The minichromosome maintenance (Mcm) 2-7 complex is the replicative helicase in eukaryotic species, and it plays essential roles in the initiation and elongation phases of DNA replication. During late M and early G(1), the Mcm2-7 complex is loaded onto chromatin to form prereplicative complex in a Cdt1-dependent manner. However, the detailed molecular mechanism of this loading process is still elusive. In this study, we demonstrate that the previously uncharacterized C-terminal domain of human Mcm6 is the Cdt1 binding domain (CBD) and present its high resolution NMR structure. The structure of CBD exhibits a typical "winged helix" fold that is generally involved in protein-nucleic acid interaction. Nevertheless, the CBD failed to interact with DNA in our studies, indicating that it is specific for protein-protein interaction. The CBD-Cdt1 interaction involves the helix-turn-helix motif of CBD. The results reported here provide insight into the molecular mechanism of Mcm2-7 chromatin loading and prereplicative complex assembly.
PubMed: 20202939
DOI: 10.1074/jbc.C109.094599
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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