4enz

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'''Unreleased structure'''
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{{STRUCTURE_4enz| PDB=4enz | SCENE= }}
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===Structure of human ceruloplasmin at 2.6 A resolution===
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The entry 4enz is ON HOLD until Paper Publication
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==Disease==
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[[http://www.uniprot.org/uniprot/CERU_HUMAN CERU_HUMAN]] Defects in CP are the cause of aceruloplasminemia (ACERULOP) [MIM:[http://omim.org/entry/604290 604290]]. It is an autosomal recessive disorder of iron metabolism characterized by iron accumulation in the brain as well as visceral organs. Clinical features consist of the triad of retinal degeneration, diabetes mellitus and neurological disturbances. Note=Ceruloplasmin levels are decreased in Wilson disease, in which copper cannot be incorporated into ceruloplasmin in liver because of defects in the copper-transporting ATPase 2.
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Authors: Samygina, V.R., Sokolov, A.V., Bourenkov, G., Vasilyev, V.B., Bartunik, H.
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==Function==
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[[http://www.uniprot.org/uniprot/CERU_HUMAN CERU_HUMAN]] Ceruloplasmin is a blue, copper-binding (6-7 atoms per molecule) glycoprotein. It has ferroxidase activity oxidizing Fe(2+) to Fe(3+) without releasing radical oxygen species. It is involved in iron transport across the cell membrane. Provides Cu(2+) ions for the ascorbate-mediated deaminase degradation of the heparan sulfate chains of GPC1. May also play a role in fetal lung development or pulmonary antioxidant defense (By similarity).
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Description: Structure of human ceruloplasmin at 2.6 A resolution
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==About this Structure==
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[[4enz]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ENZ OCA].
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[[Category: Ferroxidase]]
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[[Category: Homo sapiens]]
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[[Category: Bartunik, H.]]
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[[Category: Bourenkov, G.]]
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[[Category: Samygina, V R.]]
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[[Category: Sokolov, A V.]]
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[[Category: Vasilyev, V B.]]
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[[Category: Oxidoreductase]]
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[[Category: Plastocyanin-like domain]]

Revision as of 20:32, 17 April 2013

Template:STRUCTURE 4enz

Contents

Structure of human ceruloplasmin at 2.6 A resolution

Disease

[CERU_HUMAN] Defects in CP are the cause of aceruloplasminemia (ACERULOP) [MIM:604290]. It is an autosomal recessive disorder of iron metabolism characterized by iron accumulation in the brain as well as visceral organs. Clinical features consist of the triad of retinal degeneration, diabetes mellitus and neurological disturbances. Note=Ceruloplasmin levels are decreased in Wilson disease, in which copper cannot be incorporated into ceruloplasmin in liver because of defects in the copper-transporting ATPase 2.

Function

[CERU_HUMAN] Ceruloplasmin is a blue, copper-binding (6-7 atoms per molecule) glycoprotein. It has ferroxidase activity oxidizing Fe(2+) to Fe(3+) without releasing radical oxygen species. It is involved in iron transport across the cell membrane. Provides Cu(2+) ions for the ascorbate-mediated deaminase degradation of the heparan sulfate chains of GPC1. May also play a role in fetal lung development or pulmonary antioxidant defense (By similarity).

About this Structure

4enz is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.

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OCA

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