1ag2

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{{Seed}}
 
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[[Image:1ag2.png|left|200px]]
 
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==PRION PROTEIN DOMAIN PRP(121-231) FROM MOUSE, NMR, 2 MINIMIZED AVERAGE STRUCTURE==
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The line below this paragraph, containing "STRUCTURE_1ag2", creates the "Structure Box" on the page.
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<StructureSection load='1ag2' size='340' side='right'caption='[[1ag2]]' 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'>[[1ag2]] 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=1AG2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AG2 FirstGlance]. <br>
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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, 1 model</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=1ag2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ag2 OCA], [https://pdbe.org/1ag2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ag2 RCSB], [https://www.ebi.ac.uk/pdbsum/1ag2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ag2 ProSAT]</span></td></tr>
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{{STRUCTURE_1ag2| PDB=1ag2 | 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/ag/1ag2_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=1ag2 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 'protein only' hypothesis states that a modified form of normal prion protein triggers infectious neurodegenerative diseases, such as bovine spongiform encephalopathy (BSE), or Creutzfeldt-Jakob disease (CJD) in humans. Prion proteins are thought to exist in two different conformations: the 'benign' PrPcform, and the infectious 'scrapie form', PrPsc. Knowledge of the three-dimensional structure of PrPc is essential for understanding the transition to PrPsc. The nuclear magnetic resonance (NMR) structure of the autonomously folding PrP domain comprising residues 121-231 (ref. 6) contains a two-stranded antiparallel beta-sheet and three alpha-helices. This domain contains most of the point-mutation sites that have been linked, in human PrP, to the occurrence of familial prion diseases. The NMR structure shows that these mutations occur within, or directly adjacent to, regular secondary structures. The presence of a beta-sheet in PrP(121-231) is in contrast with model predictions of an all-helical structure of PrPc (ref. 8), and may be important for the initiation of the transition from PrPc to PrPsc.
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===PRION PROTEIN DOMAIN PRP(121-231) FROM MOUSE, NMR, 2 MINIMIZED AVERAGE STRUCTURE===
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NMR structure of the mouse prion protein domain PrP(121-321).,Riek R, Hornemann S, Wider G, Billeter M, Glockshuber R, Wuthrich K Nature. 1996 Jul 11;382(6587):180-2. PMID:8700211<ref>PMID:8700211</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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The line below this paragraph, {{ABSTRACT_PUBMED_8700211}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1ag2" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 8700211 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_8700211}}
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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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1AG2 is a 1 chain 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=1AG2 OCA].
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==Reference==
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<ref group="xtra">PMID:8700211</ref><references group="xtra"/>
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[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: Billeter, M.]]
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[[Category: Billeter M]]
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[[Category: Glockshuber, R.]]
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[[Category: Glockshuber R]]
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[[Category: Hornemann, S.]]
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[[Category: Hornemann S]]
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[[Category: Riek, R.]]
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[[Category: Riek R]]
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[[Category: Wider, G.]]
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[[Category: Wider G]]
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[[Category: Wuthrich, K.]]
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[[Category: Wuthrich K]]
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[[Category: Brain]]
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[[Category: Glycoprotein]]
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[[Category: Gpi-anchor]]
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[[Category: Prion protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 00:55:16 2009''
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Current revision

PRION PROTEIN DOMAIN PRP(121-231) FROM MOUSE, NMR, 2 MINIMIZED AVERAGE STRUCTURE

PDB ID 1ag2

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