1H, 15N and 13C chemical shift assignments of the Cdt1 binding domain of human Mcm6

Biomolecular NMR Assignments
Changdong LiuGuang Zhu

Abstract

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).

References

Nov 1, 1995·Journal of Biomolecular NMR·F DelaglioA Bax
Feb 21, 1998·Trends in Biotechnology·G M Clore, A M Gronenborn
Mar 10, 2004·Microbiology and Molecular Biology Reviews : MMBR·Susan L Forsburg
Jan 18, 2005·Nucleic Acids Research·Andrew FerenbachJ Julian Blow

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