1H, 15N and 13C chemical shift assignments of the Cdt1 binding domain of human Mcm6.
The eukaryotic minichromsome maintenance (Mcm) proteins (Mcm2-7) are evolutionally conserved from yeast to human. These proteins are essential for DNA replication and Mcm6 is one subunit of Mcm2-7 complex that serves as the replicative helicase in DNA replication. Cdt1 is a critical member of pre-replicative complex (pre-RC), which directs the chromatin loading of Mcm2-7 complex. The Cdt1 binding domain (CBD) of human Mcm6 was found to directly interact with Cdt1 and this interaction may mediate the chromatin loading of Mcm2-7 complex. The structure of CBD exhibits a typical "winged-helix" fold which is generally involved in protein-nucleic acid interaction. Here we report the (1)H, (15)N and (13)C chemical shift assignments of human Mcm6 CBD determined by triple resonance experiments. The resonance assignments obtained in this work were required for the structure-function studies of CBD by NMR spectroscopy (BMRB deposits with accession number 16396).
Liu
Changdong
C
Department of Physics and Shanghai Key Laboratory for Magnetic Resonance, East China Normal University, Shanghai, 200062, China.
Wei
Zhun
Z
Zhu
Guang
G
D002247:Carbon Isotopes; D018797:Cell Cycle Proteins / Q000737:chemistry* / Q000378:metabolism*; D006801:Humans; D006859:Hydrogen; D064151:Minichromosome Maintenance Complex Component 6; D009587:Nitrogen Isotopes; D019906:Nuclear Magnetic Resonance, Biomolecular; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary
C467199:CDT1 protein, human; D002247:Carbon Isotopes; D018797:Cell Cycle Proteins; D009587:Nitrogen Isotopes; D006859:Hydrogen; C103258:MCM6 protein, human; D064151:Minichromosome Maintenance Complex Component 6