| 词条 | CD59 antigen |
| 释义 |
| Symbol = UPAR_LY6 | Name = u-PAR/Ly-6 domain | image = Cd59b.png | width = | caption = Crystallographic structure of non-glycosylated human CD59.[1] | Pfam= PF00021 | InterPro= IPR001526 | SMART= | Prosite = PDOC00756 | SCOP = 1erg | TCDB = | OPM family= | OPM protein= | CDD = cd00117 | PDB={{PDB3|1cds}} :28-95 {{PDB3|1cdr}} :28-95 {{PDB3|1cdq}} :28-95{{PDB3|1erg}} :28-95 {{PDB3|1ywh}}C:25-99 {{PDB3|1vye}}A:23-80 }} CD59 antigen (also called 1F-5Ag, H19, HRF20, MACIF, MIRL, P-18 or protectin) inhibits formation of membrane attack complex (MAC), thus protecting cells from complement-mediated lysis. It has a signaling role, as a GPI anchored molecule, in T cell activation and appears to have some role in cell adhesion through CD2 (controversial). CD59 associates with C9, inhibiting incorporation into C5b-8 preventing terminal steps in polymerization of the (MAC) in plasma membranes. Genetic defects in GPI-anchor attachment that cause a reduction or loss of both CD59 and CD55 on erythrocytes produce the symptoms of the disease paroxysmal nocturnal hemoglobinuria (PNH). A variety of GPI-linked cell-surface glycoproteins are composed of one or more copies of a conserved domain of about 100 amino-acid residues.[2][3] Among these proteins, U-PAR contains three tandem copies of the domain, while all the others are made up of a single domain. As shown in the following schematic, this conserved domain contains 10 cysteine residues involved in five disulfide bonds - in U-PAR, the first copy of the domain lacks the fourth disulfide bond. | | | | | | | | | | 'C': conserved cysteine involved in a disulfide bond. CD molecules are leucocyte antigens on cell surfaces. CD antigens nomenclature is updated at Protein Reviews On The Web (http://mpr.nci.nih.gov/prow/). Subfamilies
Human proteins containing this domainARS; CD177; CD59; LY6D; LY6E; LY6H; LYNX1; LYPD2; LYPD3; LYPD4; LYPD5; LYPD6; PLAUR; PSCA; SLURP2; SLURP1; SPACA4; TEX101; References1. ^{{PDB|2J8B}}; {{cite journal |vauthors=Leath KJ, Johnson S, Roversi P, Hughes TR, Smith RA, Mackenzie L, Morgan BP, Lea SM | title = High-resolution structures of bacterially expressed soluble human CD59 | journal = Acta Crystallographica Section F | volume = 63 | issue = Pt 8 | pages = 648–52 |date=August 2007 | pmid = 17671359 | pmc = 2335151 | doi = 10.1107/S1744309107033477 | url = | issn = }} {{InterPro content|IPR001526}}{{DEFAULTSORT:Cd59 Antigen}}2. ^{{cite journal |vauthors=Patthy L, Blasi F, Behrendt N, Ploug M, Houen G, Dano K |title=The ligand-binding domain of the cell surface receptor for urokinase-type plasminogen activator |journal=J. Biol. Chem. |volume=266 |issue=12 |pages=7842–7847 |year=1991 |pmid=1850423}} 3. ^{{cite journal |vauthors=Ploug M, Dano K, Kjalke M, Ronne E, Weidle U, Hoyer-Hansen G |title=Localization of the disulfide bonds in the NH2-terminal domain of the cellular receptor for human urokinase-type plasminogen activator. A domain structure belonging to a novel superfamily of glycolipid-anchored membrane proteins |journal=J. Biol. Chem. |volume=268 |issue=23 |pages=17539–17546 |year=1993 |pmid=8394346}} 3 : Protein domains|Membrane proteins|Blood antigen systems |
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