Crystal structure of human CDC7 kinase in complex with its activator DBF4 View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2012-11

AUTHORS

Siobhan Hughes, Frédéric Elustondo, Andrea Di Fonzo, Frédéric G Leroux, Ai C Wong, Ambrosius P Snijders, Stephen J Matthews, Peter Cherepanov

ABSTRACT

CDC7 is a serine/threonine kinase that is essential for the initiation of eukaryotic DNA replication. CDC7 activity is controlled by its activator, DBF4. Here we present crystal structures of human CDC7-DBF4 in complex with a nucleotide or ATP-competing small molecules, revealing the active and inhibited forms of the kinase, respectively. DBF4 wraps around CDC7, burying approximately 6,000 Å(2) of hydrophobic molecular surface in a bipartite interface. The effector domain of DBF4, containing conserved motif C, is essential and sufficient to support CDC7 kinase activity by binding to the kinase N-terminal lobe and stabilizing its canonical αC helix. DBF4 motif M latches onto the C-terminal lobe of the kinase, acting as a tethering domain. Our results elucidate the structural basis for binding to and activation of CDC7 by DBF4 and provide a framework for the design of more potent and specific CDC7 inhibitors. More... »

PAGES

1101

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/nsmb.2404

DOI

http://dx.doi.org/10.1038/nsmb.2404

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1019162678

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/23064647


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