7yat
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[7yat]] is a 24 chain structure with sequence from [https://en.wikipedia.org/wiki/Mesocricetus_auratus Mesocricetus auratus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7YAT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7YAT FirstGlance]. <br> | <table><tr><td colspan='2'>[[7yat]] is a 24 chain structure with sequence from [https://en.wikipedia.org/wiki/Mesocricetus_auratus Mesocricetus auratus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7YAT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7YAT FirstGlance]. <br> | ||
| - | </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=7yat FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7yat OCA], [https://pdbe.org/7yat PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7yat RCSB], [https://www.ebi.ac.uk/pdbsum/7yat PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7yat ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.2Å</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=7yat FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7yat OCA], [https://pdbe.org/7yat PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7yat RCSB], [https://www.ebi.ac.uk/pdbsum/7yat PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7yat ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Disease == | == Disease == | ||
| - | + | [https://www.uniprot.org/uniprot/PRIO_MESAU PRIO_MESAU] 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. | |
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/PRIO_MESAU PRIO_MESAU] 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).<ref>PMID:19059915</ref> | |
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Fibrils of the hamster prion peptide (sHaPrP, sequence 108-144) were prepared in an acidic solution, and their structure was solved by cryogenic electron microscopy with a resolution of 2.23 A based on the gold-standard Fourier shell correlation (FSC) curve. The fibril has a novel architecture that has never been found in other amyloid fibrils. Each fibril is assembled by four protofilaments (PFs) and has an ordered water channel in the center. Each protofilament contains three beta-strands (125-130, 133-135, and 138-141) arranged in an "R"-shaped construct. The structural data indicate that these three beta-strand segments are the most amyloidogenic region of the prion peptide/protein and might be the site of nucleation during fibrillization under conditions without denaturants. | Fibrils of the hamster prion peptide (sHaPrP, sequence 108-144) were prepared in an acidic solution, and their structure was solved by cryogenic electron microscopy with a resolution of 2.23 A based on the gold-standard Fourier shell correlation (FSC) curve. The fibril has a novel architecture that has never been found in other amyloid fibrils. Each fibril is assembled by four protofilaments (PFs) and has an ordered water channel in the center. Each protofilament contains three beta-strands (125-130, 133-135, and 138-141) arranged in an "R"-shaped construct. The structural data indicate that these three beta-strand segments are the most amyloidogenic region of the prion peptide/protein and might be the site of nucleation during fibrillization under conditions without denaturants. | ||
| - | 2.2 A Cryo-EM Tetra-Protofilament Structure of the Hamster Prion 108-144 Fibril Reveals an Ordered Water Channel in the Center.,Chen EH, Kao HW, Lee CH, Huang JYC, Wu KP, Chen RP J Am Chem Soc. 2022 | + | 2.2 A Cryo-EM Tetra-Protofilament Structure of the Hamster Prion 108-144 Fibril Reveals an Ordered Water Channel in the Center.,Chen EH, Kao HW, Lee CH, Huang JYC, Wu KP, Chen RP J Am Chem Soc. 2022 Aug 3;144(30):13888-13894. doi: 10.1021/jacs.2c05479. Epub , 2022 Jul 20. PMID:35857020<ref>PMID:35857020</ref> |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 7yat" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 7yat" style="background-color:#fffaf0;"></div> | ||
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| + | ==See Also== | ||
| + | *[[Prion 3D structures|Prion 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
Current revision
CryoEM tetra protofilament structure of the hamster prion 108-144 fibril
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