Ceruloplasmin

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{{STRUCTURE_1kcw| PDB=1kcw | SIZE=400| SCENE= |right|CAPTION=Human ceruloplasmin complex with Cu+2 ions, [[1kcw]] }}
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<StructureSection load='1kcw' size='350' side='right' caption='Glycosylated human ceruloplasmin complex with Cu+2 ions (orange) and O atoms (red) (PDB entry [[1kcw]])' scene='46/467272/Cv/2'>
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__TOC__
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== Function ==
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'''Ceruloplasmin''' (CP) is a ferroxidase which is the major copper-carrying protein in the blood. It functions in iron metabolism.
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'''Ceruloplasmin''' (CP) is a ferroxidase which is the major copper-carrying protein in the blood. It functions in iron metabolism.<ref>PMID:12055353</ref>
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{{TOC limit|limit=2}}
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== Relevance ==
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CP testing is used in diagnosis of the rare inherited disorder - Wilson disease.
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== Disease ==
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CP mutation causes the autosomal recessive disorder - Aceruloplasminemia which results in accumulation of iron in the brain.
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== Structural highlights ==
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<scene name='46/467272/Cv/8'>Cu-O-Cu coordination site</scene> and
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<scene name='46/467272/Cv/9'>Cu-O coordination site</scene> in human ceruloplasmin (PDB entry [[1kcw]]).
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</StructureSection>
==3D structures of ceruloplasmin==
==3D structures of ceruloplasmin==
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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
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[[1kcw]], [[2j5w]] – hCP - human
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[[1kcw]], [[2j5w]], [[4enz]] – hCP - human<br />
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[[4ejx]] – hCP + myeloperoxidase<br />
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[[5n0k]], [[5n4l]] – CP – rat<br />
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== References ==
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<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Current revision

Glycosylated human ceruloplasmin complex with Cu+2 ions (orange) and O atoms (red) (PDB entry 1kcw)

Drag the structure with the mouse to rotate

3D structures of ceruloplasmin

Updated on 11-February-2019

1kcw, 2j5w, 4enz – hCP - human
4ejx – hCP + myeloperoxidase
5n0k, 5n4l – CP – rat

References

  1. Hellman NE, Gitlin JD. Ceruloplasmin metabolism and function. Annu Rev Nutr. 2002;22:439-58. Epub 2002 Apr 4. PMID:12055353 doi:http://dx.doi.org/10.1146/annurev.nutr.22.012502.114457

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Michal Harel, Alexander Berchansky

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