1y15

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{{Seed}}
 
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[[Image:1y15.png|left|200px]]
 
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==Mouse Prion Protein with mutation N174T==
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The line below this paragraph, containing "STRUCTURE_1y15", creates the "Structure Box" on the page.
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<StructureSection load='1y15' size='340' side='right'caption='[[1y15]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1y15]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y15 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Y15 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1y15 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y15 OCA], [https://pdbe.org/1y15 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1y15 RCSB], [https://www.ebi.ac.uk/pdbsum/1y15 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1y15 ProSAT]</span></td></tr>
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{{STRUCTURE_1y15| PDB=1y15 | SCENE= }}
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</table>
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== Disease ==
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[https://www.uniprot.org/uniprot/PRIO_MOUSE PRIO_MOUSE] Note=Found in high quantity in the brain of humans and animals infected with degenerative neurological diseases such as kuru, Creutzfeldt-Jakob disease (CJD), Gerstmann-Straussler syndrome (GSS), scrapie, bovine spongiform encephalopathy (BSE), transmissible mink encephalopathy (TME), etc.
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== Function ==
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[https://www.uniprot.org/uniprot/PRIO_MOUSE PRIO_MOUSE] 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) (By similarity). 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.<ref>PMID:12732622</ref> <ref>PMID:16492732</ref> <ref>PMID:19242475</ref> <ref>PMID:19568430</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/y1/1y15_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1y15 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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===Mouse Prion Protein with mutation N174T===
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1y15" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_15647363}}, adds the Publication Abstract to the page
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*[[Prion 3D structures|Prion 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 15647363 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_15647363}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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1Y15 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y15 OCA].
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==Reference==
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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:[http://www.ncbi.nlm.nih.gov/pubmed/15647363 15647363]
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[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: Single protein]]
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[[Category: Bonjour S]]
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[[Category: Bonjour, S.]]
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[[Category: Fiorito F]]
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[[Category: Fiorito, F.]]
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[[Category: Gossert AD]]
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[[Category: Gossert, A D.]]
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[[Category: Lysek DA]]
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[[Category: Lysek, D A.]]
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[[Category: Wuthrich K]]
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[[Category: Wuthrich, K.]]
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[[Category: Cwd]]
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[[Category: Nmr]]
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[[Category: Prion protein]]
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[[Category: Prp]]
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[[Category: Tse]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 21:34:02 2008''
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Current revision

Mouse Prion Protein with mutation N174T

PDB ID 1y15

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