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M513667200v1
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Papers In Press, published online ahead of print April 20, 2006
J. Biol. Chem, 10.1074/jbc.M513667200
Submitted on December 22, 2005
Accepted on April 20, 2006

The structure of the human centrin 2-xeroderma pigmentosum group C protein complex

James R Thompson, Zachary C Ryan, Jeffery L Salisbury, and Rajiv Kumar

Department of Physiology and Biomedical Engineering, Mayo Clinic School of Medicine, Rochester, MN 55905

Corresponding Author: thompson.james{at}mayo.edu

Human centrin-2 plays a key role in centrosome function and stimulates nucleotide excision repair by binding to the xeroderma pigmentosum group C protein. To determine the structure of human centrin-2 and to develop an understanding of molecular interactions between centrin and xeroderma pigmentosum group C protein, we characterized the crystal structure of calcium-loaded full-length centrin 2 complexed with a xeroderma pigmentosum group C peptide. Our structure shows that the carboxy terminal domain of centrin-2 binds this peptide and two calcium atoms, while the amino terminal lobe is in a closed conformation positioned distantly by an ordered a-helical linker. A stretch of the amino terminal domain unique to centrins appears disordered. Two xeroderma pigmentosum group C peptides both bound to centrin-2 also interact to form an a helical coiled-coil. The interface between centrin-2 and each peptide is predominately non-polar and key hydrophobic residues of XPC have been identified that lead us to propose a novel binding motif for centrin.


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