3fod
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3fod]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FOD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FOD FirstGlance]. <br> | <table><tr><td colspan='2'>[[3fod]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FOD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FOD FirstGlance]. <br> | ||
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.4Å</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=3fod FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fod OCA], [https://pdbe.org/3fod PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3fod RCSB], [https://www.ebi.ac.uk/pdbsum/3fod PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3fod ProSAT]</span></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=3fod FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fod OCA], [https://pdbe.org/3fod PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3fod RCSB], [https://www.ebi.ac.uk/pdbsum/3fod PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3fod ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | In prion inheritance and transmission, strains are phenotypic variants encoded by protein 'conformations'. However, it is unclear how a protein conformation can be stable enough to endure transmission between cells or organisms. Here we describe new polymorphic crystal structures of segments of prion and other amyloid proteins, which offer two structural mechanisms for the encoding of prion strains. In packing polymorphism, prion strains are encoded by alternative packing arrangements (polymorphs) of beta-sheets formed by the same segment of a protein; in segmental polymorphism, prion strains are encoded by distinct beta-sheets built from different segments of a protein. Both forms of polymorphism can produce enduring conformations capable of encoding strains. These molecular mechanisms for transfer of protein-encoded information into prion strains share features with the familiar mechanism for transfer of nucleic acid-encoded information into microbial strains, including sequence specificity and recognition by noncovalent bonds. | ||
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| - | Molecular mechanisms for protein-encoded inheritance.,Wiltzius JJ, Landau M, Nelson R, Sawaya MR, Apostol MI, Goldschmidt L, Soriaga AB, Cascio D, Rajashankar K, Eisenberg D Nat Struct Mol Biol. 2009 Sep;16(9):973-8. Epub 2009 Aug 16. PMID:19684598<ref>PMID:19684598</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 3fod" style="background-color:#fffaf0;"></div> | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Eisenberg | + | [[Category: Eisenberg D]] |
| - | [[Category: Rajashankar | + | [[Category: Rajashankar K]] |
| - | [[Category: Sawaya | + | [[Category: Sawaya MR]] |
| - | [[Category: Wiltzius | + | [[Category: Wiltzius JJW]] |
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Current revision
AILSST segment from Islet Amyloid Polypeptide
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