1kcw
From Proteopedia
Contents |
X-RAY CRYSTAL STRUCTURE OF HUMAN CERULOPLASMIN AT 3.0 ANGSTROMS
Template:ABSTRACT PUBMED 009649340
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
1kcw is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.
See Also
Reference
- Machonkin TE, Zhang HH, Hedman B, Hodgson KO, Solomon EI. Spectroscopic and magnetic studies of human ceruloplasmin: identification of a redox-inactive reduced Type 1 copper site. Biochemistry. 1998 Jun 30;37(26):9570-8. PMID:9649340 doi:10.1021/bi980434v
- Villoutreix BO, Dahlback B. Structural investigation of the A domains of human blood coagulation factor V by molecular modeling. Protein Sci. 1998 Jun;7(6):1317-25. PMID:9655335 doi:10.1002/pro.5560070607
