8dja
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[8dja]] is a 20 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8DJA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8DJA FirstGlance]. <br> | <table><tr><td colspan='2'>[[8dja]] is a 20 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8DJA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8DJA 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=8dja FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8dja OCA], [https://pdbe.org/8dja PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8dja RCSB], [https://www.ebi.ac.uk/pdbsum/8dja PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8dja 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]] 3.92Å</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=8dja FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8dja OCA], [https://pdbe.org/8dja PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8dja RCSB], [https://www.ebi.ac.uk/pdbsum/8dja PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8dja ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| - | == | + | <div style="background-color:#fffaf0;"> |
| - | + | == Publication Abstract from PubMed == | |
| - | + | One of the least understood aspects of prion diseases is the structure of infectious prion protein aggregates. Here we report a high-resolution cryo-EM structure of amyloid fibrils formed by human prion protein with the Y145Stop mutation that is associated with a familial prion disease. This structural insight allows us not only to explain previous biochemical findings, but also provides direct support for the conformational adaptability model of prion transmissibility barriers. | |
| - | + | ||
| + | Cryo-EM structure of disease-related prion fibrils provides insights into seeding barriers.,Li Q, Jaroniec CP, Surewicz WK Nat Struct Mol Biol. 2022 Oct;29(10):962-965. doi: 10.1038/s41594-022-00833-4. , Epub 2022 Sep 12. PMID:36097290<ref>PMID:36097290</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 8dja" style="background-color:#fffaf0;"></div> | ||
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| + | ==See Also== | ||
| + | *[[Prion 3D structures|Prion 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
Current revision
Cryo-EM structure of mouse PrP23-144 amyloid fibrils (polymorph 1)
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