Protein Domain : IPR022416

Type:  Domain Name:  Prion/Doppel protein, beta-ribbon domain
Description:  This entry represents the C-terminal beta-ribbon domain found in prion proteins [] and the prion-like Doppel proteins []. This domain has a beta-alpha-beta-alpha(2) structure that contains an antiparallel beta-ribbon.Prion protein (PrP-c) [, , ] is a small glycoprotein found in high quantity in the brain of animals infected with certain degenerative neurological diseases, such as sheep scrapie and bovine spongiform encephalopathy (BSE), and the human dementias Creutzfeldt-Jacob disease (CJD) and Gerstmann-Straussler syndrome (GSS). PrP-c is encoded in the host genome and is expressed both in normal and infected cells. During infection, however, the PrP-c molecule become altered (conformationally rather than at the amino acid level) to an abnormal isoform, PrP-sc. In detergent-treated brain extracts from infected individuals, fibrils composed of polymers of PrP-sc, namely scrapie-associated fibrils or prion rods, can be evidenced by electron microscopy. The precise function of the normal PrP isoform in healthy individuals remains unknown. Several results, mainly obtained in transgenic animals, indicate that PrP-cmight play a role in long-term potentiation, in sleep physiology, in oxidative burst compensation (PrP can fix four Cu2+ through its octarepeat domain), in interactions with the extracellular matrix (PrP-c can bind to the precursor of the laminin receptor, LRP), in apoptosis and in signal transduction (costimulation ofPrP-c induces a modulation of Fyn kinase phosphorylation) [].The normal isoform, PrP-c, is anchored at the cell membrane, in rafts, through a glycosyl phosphatidyl inositol (GPI); its half-life at the cell surface is 5 h, after which the protein is internalised through a caveolae-dependent mechanism and degraded in the endolysosome compartment. Conversion between PrP-c and PrP-scoccurs likely during the internalisation process. In humans, PrP is a 253 amino acid protein, which has a molecular weight of 35-36 kDa. It has two hexapeptides and repeated octapeptides at the N terminus, a disulphide bond and is associated at the C terminus with a GPI, which enables it to anchor to the external part of thecell membrane. The secondary structure of PrP-c is mainly composed of alpha-helices, whereas PrP-sc is mainly beta-sheets: transconformation of alpha-helices into beta-sheets has beenproposed as the structural basis by which PrP acquires pathogenicity in TSEs. The three-dimensional structures shows the protein to be made of a globular domain which includes three alpha-helices and two small antiparallel beta-sheet structures, and a long flexible tail whose conformation depends on the biophysical parameters of the environment. Crystals of the globular domain of PrPhave recently been obtained; their analysis suggests a possible dimerisation of the protein through the three-dimensional swapping of the C-terminal helix 3 and rearrangement of the disulphide bond. Short Name:  Prion/Doppel_prot_b-ribbon_dom

0 Child Features

0 Contains

5 Cross Referencess

Identifier
PF00377
PS00291
PS00706
G3DSA:1.10.790.10
SSF54098

1 Found In

DB identifier Type Name
IPR000817 Family Prion protein

2 GO Annotations

GO Term Gene Name
GO:0051260 IPR022416
GO:0016020 IPR022416

2 Ontology Annotations

GO Term Gene Name
GO:0051260 IPR022416
GO:0016020 IPR022416

0 Parent Features

305 Proteins

DB identifier UniProt Accession Secondary Identifier Organism Name Length
evm.model.supercontig_170.29 PAC:16410848 Carica papaya 530  
29917.m002022 B9S669 PAC:16813625 Ricinus communis 513  
orange1.1g016907m A0A067G0W2 PAC:18138354 Citrus sinensis 380  
orange1.1g016899m A0A067G0W2 PAC:18138353 Citrus sinensis 380  
AT4G16200.1 O23467 PAC:19646709 Arabidopsis thaliana 288  
Lus10013793 PAC:23169135 Linum usitatissimum 332  
Lus10008744 PAC:23169030 Linum usitatissimum 546  
Lus10039139 PAC:23150399 Linum usitatissimum 339  
Potri.002G135900.1 A0A2K2BIC7 PAC:27022275 Populus trichocarpa 95  
Gorai.006G049800.1 A0A0D2NM14 PAC:26830672 Gossypium raimondii 275  
60407 C1MY55 PAC:27338894 Micromonas pusilla CCMP1545 625  
Thecc1EG015225t1 A0A061G8B6 PAC:27449574 Theobroma cacao 277  
Thecc1EG019733t1 A0A061EHZ3 PAC:27451950 Theobroma cacao 393  
Araha.9898s0003.1.p PAC:28854232 Arabidopsis halleri 89  
Glyma.16G042200.2.p K7MF58 PAC:30558988 Glycine max 282  
Brara.G00921.1.p A0A397YRU7 PAC:30635064 Brassica rapa FPsc 191  
Medtr4g020000.1 A0A072UGW1 PAC:31107915 Medicago truncatula 358  
Medtr7g085420.1 A2Q5Q1 PAC:31080081 Medicago truncatula 273  
Spipo4G0041300 PAC:31504141 Spirodela polyrhiza 696  
Spipo1G0053000 PAC:31521204 Spirodela polyrhiza 301  
Traes_2BL_D1A2A798A.1 PAC:31791853 Triticum aestivum 112  
Traes_2BS_0B287DC6C.1 PAC:31789609 Triticum aestivum 330  
Traes_3B_542506C38.2 PAC:31768593 Triticum aestivum 602  
Traes_3B_542506C38.3 PAC:31768594 Triticum aestivum 602  
Traes_3B_542506C38.1 PAC:31768595 Triticum aestivum 438  
Traes_4AL_2028C436C.1 PAC:31742582 Triticum aestivum 99  
Traes_5DL_E1134AE11.2 PAC:31862135 Triticum aestivum 418  
Traes_6DS_B73B70A62.4 PAC:32023044 Triticum aestivum 102  
Traes_6DS_B73B70A62.2 PAC:32023045 Triticum aestivum 102  
Traes_6DS_B73B70A62.3 PAC:32023046 Triticum aestivum 102  

6 Publications

First Author Title Year Journal Volume Pages PubMed ID
            2572197
            1916104
            2908696
            12354606
            11524679
            12595265