2ggm
From Proteopedia
Human centrin 2 xeroderma pigmentosum group C protein complex
Overview
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 carboxyl-terminal domain of centrin-2 binds this peptide and two calcium atoms, whereas the amino-terminal lobe is in a closed conformation positioned distantly by an ordered alpha-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 alpha-helical coiled-coil. The interface between centrin-2 and each peptide is predominantly nonpolar, and key hydrophobic residues of XPC have been identified that lead us to propose a novel binding motif for centrin.
About this Structure
2GGM is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The structure of the human centrin 2-xeroderma pigmentosum group C protein complex., Thompson JR, Ryan ZC, Salisbury JL, Kumar R, J Biol Chem. 2006 Jul 7;281(27):18746-52. Epub 2006 Apr 20. PMID:16627479 Page seeded by OCA on Sun May 4 05:05:07 2008
