2ggm
From Proteopedia
(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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| - | [[Image:2ggm.gif|left|200px]]<br /> | + | [[Image:2ggm.gif|left|200px]]<br /><applet load="2ggm" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="2ggm" size=" | + | |
caption="2ggm, resolution 2.35Å" /> | caption="2ggm, resolution 2.35Å" /> | ||
'''Human centrin 2 xeroderma pigmentosum group C protein complex'''<br /> | '''Human centrin 2 xeroderma pigmentosum group C protein complex'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Human centrin-2 plays a key role in centrosome function and stimulates | + | 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== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2GGM is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 2GGM is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GGM OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Thompson, J | + | [[Category: Thompson, J R.]] |
[[Category: CA]] | [[Category: CA]] | ||
[[Category: dna repair complex]] | [[Category: dna repair complex]] | ||
[[Category: ef-hand superfamily]] | [[Category: ef-hand superfamily]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:31:35 2008'' |
Revision as of 15:31, 21 February 2008
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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 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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