2klq | pdb_00002klq
From Proteopedia
The solution structure of CBD of human MCM6
| ||||||||||||
Structural highlights
Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. Characterization and structure determination of the Cdt1 binding domain of human minichromosome maintenance (Mcm) 6.,Wei Z, Liu C, Wu X, Xu N, Zhou B, Liang C, Zhu G J Biol Chem. 2010 Apr 23;285(17):12469-73. Epub 2010 Mar 4. PMID:20202939[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
Contents | ||||||||||||||||
This page was last modified 08:01, 30 September 2014.