6dso

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<SX load='6dso' size='340' side='right' viewer='molstar' caption='[[6dso]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
<SX load='6dso' size='340' side='right' viewer='molstar' caption='[[6dso]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6dso]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6DSO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6DSO FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6dso]] is a 12 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=6DSO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6DSO FirstGlance]. <br>
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</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6dso FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6dso OCA], [http://pdbe.org/6dso PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6dso RCSB], [http://www.ebi.ac.uk/pdbsum/6dso PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6dso ProSAT]</span></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3&#8491;</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=6dso FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6dso OCA], [https://pdbe.org/6dso PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6dso RCSB], [https://www.ebi.ac.uk/pdbsum/6dso PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6dso ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
== Disease ==
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[[http://www.uniprot.org/uniprot/SAA2_MOUSE SAA2_MOUSE]] Reactive, secondary amyloidosis is characterized by the extracellular accumulation in various tissues of the SAA protein. These deposits are highly insoluble and resistant to proteolysis; they disrupt tissue structure and compromise function.
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[https://www.uniprot.org/uniprot/SAA2_MOUSE SAA2_MOUSE] Reactive, secondary amyloidosis is characterized by the extracellular accumulation in various tissues of the SAA protein. These deposits are highly insoluble and resistant to proteolysis; they disrupt tissue structure and compromise function.
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/SAA2_MOUSE SAA2_MOUSE]] Major acute phase reactant. Apolipoprotein of the HDL complex.
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[https://www.uniprot.org/uniprot/SAA2_MOUSE SAA2_MOUSE] Major acute phase reactant. Apolipoprotein of the HDL complex.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Systemic AA amyloidosis is a worldwide occurring protein misfolding disease of humans and animals. It arises from the formation of amyloid fibrils from the acute phase protein serum amyloid A. Here, we report the purification and electron cryo-microscopy analysis of amyloid fibrils from a mouse and a human patient with systemic AA amyloidosis. The obtained resolutions are 3.0 A and 2.7 A for the murine and human fibril, respectively. The two fibrils differ in fundamental properties, such as presence of right-hand or left-hand twisted cross-beta sheets and overall fold of the fibril proteins. Yet, both proteins adopt highly similar beta-arch conformations within the N-terminal ~21 residues. Our data demonstrate the importance of the fibril protein N-terminus for the stability of the analyzed amyloid fibril morphologies and suggest strategies of combating this disease by interfering with specific fibril polymorphs.
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Cryo-EM fibril structures from systemic AA amyloidosis reveal the species complementarity of pathological amyloids.,Liberta F, Loerch S, Rennegarbe M, Schierhorn A, Westermark P, Westermark GT, Hazenberg BPC, Grigorieff N, Fandrich M, Schmidt M Nat Commun. 2019 Mar 7;10(1):1104. doi: 10.1038/s41467-019-09033-z. PMID:30846696<ref>PMID:30846696</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 6dso" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
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[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: Fandrich, M]]
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[[Category: Fandrich M]]
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[[Category: Grigorieff, N]]
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[[Category: Grigorieff N]]
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[[Category: Liberta, F]]
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[[Category: Liberta F]]
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[[Category: Loerch, S]]
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[[Category: Loerch S]]
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[[Category: Schmidt, M]]
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[[Category: Schmidt M]]
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[[Category: Aa-amyloidosis]]
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[[Category: Cross-beta]]
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[[Category: Fibril]]
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[[Category: Helical]]
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[[Category: Protein fibril]]
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Current revision

Cryo-EM structure of murine AA amyloid fibril

6dso, resolution 3.00Å

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OCA

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