1xyw
From Proteopedia
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| - | {{STRUCTURE_1xyw| PDB=1xyw | SCENE= }} | ||
| - | ===elk prion protein=== | ||
| - | {{ABSTRACT_PUBMED_15647363}} | ||
| - | == | + | ==elk prion protein== |
| - | [[http://www.uniprot.org/uniprot/PRIO_CEREN PRIO_CEREN | + | <StructureSection load='1xyw' size='340' side='right'caption='[[1xyw]]' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1xyw]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Cervus_canadensis_nelsoni Cervus canadensis nelsoni]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XYW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XYW FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1xyw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xyw OCA], [https://pdbe.org/1xyw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xyw RCSB], [https://www.ebi.ac.uk/pdbsum/1xyw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xyw ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Disease == | ||
| + | [https://www.uniprot.org/uniprot/PRIO_CEREN PRIO_CEREN] Note=PrP is found in high quantity in the brain of humans and animals infected with the degenerative neurological diseases kuru, Creutzfeldt-Jakob disease (CJD), Gerstmann-Straussler syndrome (GSS), scrapie, bovine spongiform encephalopathy (BSE), transmissible mink encephalopathy (TME), etc. | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/PRIO_CEREN PRIO_CEREN] May play a role in neuronal development and synaptic plasticity. May be required for neuronal myelin sheath maintenance. May play a role in iron uptake and iron homeostasis. Soluble oligomers are toxic to cultured neuroblastoma cells and induce apoptosis (in vitro). Association with GPC1 (via its heparan sulfate chains) targets PRNP to lipid rafts. Also provides Cu(2+) or ZN(2+) for the ascorbate-mediated GPC1 deaminase degradation of its heparan sulfate side chains (By similarity). | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/xy/1xyw_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1xyw ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The NMR structure of the recombinant elk prion protein (ePrP), which represents the cellular isoform (ePrPC) in the healthy organism, is described here. As anticipated from the highly conserved amino acid sequence, ePrPC has the same global fold as other mammalian prion proteins (PrPs), with a flexibly disordered "tail" of residues 23-124 and a globular domain 125-226 with three alpha-helices and a short antiparallel beta-sheet. However, ePrPC shows a striking local structure variation when compared with most other mammalian PrPs, in particular human, bovine, and mouse PrPC. A loop of residues 166-175, which links the beta-sheet with the alpha2-helix and is part of a hypothetical "protein X" epitope, is outstandingly well defined, whereas this loop is disordered in the other species. Based on NMR structure determinations of two mouse PrP variants, mPrP[N174T] and mPrP[S170N,N174T], this study shows that the structured loop in ePrPC relates to these two local amino acid exchanges, so that mPrP[S170N,N174T] exactly mimics ePrPC. These results are evaluated in the context of recent reports on chronic wasting disease (CWD) in captive and free-ranging deer and elk in the U.S. and Canada, and an animal model is proposed for support of future research on CWD. | ||
| - | + | Prion protein NMR structures of elk and of mouse/elk hybrids.,Gossert AD, Bonjour S, Lysek DA, Fiorito F, Wuthrich K Proc Natl Acad Sci U S A. 2005 Jan 18;102(3):646-50. Epub 2005 Jan 12. PMID:15647363<ref>PMID:15647363</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| + | <div class="pdbe-citations 1xyw" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
| - | *[[Prion|Prion]] | + | *[[Prion 3D structures|Prion 3D structures]] |
| - | + | == References == | |
| - | == | + | <references/> |
| - | + | __TOC__ | |
| - | [[Category: Cervus | + | </StructureSection> |
| - | [[Category: Bonjour | + | [[Category: Cervus canadensis nelsoni]] |
| - | [[Category: Fiorito | + | [[Category: Large Structures]] |
| - | [[Category: Gossert | + | [[Category: Bonjour S]] |
| - | [[Category: Lysek | + | [[Category: Fiorito F]] |
| - | [[Category: Wuthrich | + | [[Category: Gossert AD]] |
| - | + | [[Category: Lysek DA]] | |
| - | + | [[Category: Wuthrich K]] | |
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Current revision
elk prion protein
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