2ggm
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(New page: 200px<br /> <applet load="2ggm" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ggm, resolution 2.35Å" /> '''Human centrin 2 xer...)
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Revision as of 20:12, 12 November 2007
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Human centrin 2 xeroderma pigmentosum group C protein complex
Contents |
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.
Disease
Known diseases associated with this structure: Xeroderma pigmentosum, group C OMIM:[278720]
About this Structure
2GGM is a Protein complex structure of sequences from Homo sapiens with CA as ligand. 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
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