6zrf
From Proteopedia
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==amyloid structure of amylin (IAPP - islet amyloid polypeptide)== | ==amyloid structure of amylin (IAPP - islet amyloid polypeptide)== | ||
| - | <StructureSection load='6zrf' size='340' side='right'caption='[[6zrf]]' scene=''> | + | <StructureSection load='6zrf' size='340' side='right'caption='[[6zrf]], [[Resolution|resolution]] 3.60Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ZRF OCA]. For a <b>guided tour on the structure components</b> use [ | + | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ZRF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6ZRF FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.6Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=TYC:L-TYROSINAMIDE'>TYC</scene></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=6zrf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6zrf OCA], [https://pdbe.org/6zrf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6zrf RCSB], [https://www.ebi.ac.uk/pdbsum/6zrf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6zrf ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Aggregation of the peptide hormone amylin into amyloid deposits is a pathological hallmark of type-2 diabetes (T2D). While no causal link between T2D and amyloid has been established, the S20G mutation in amylin is associated with early-onset T2D. Here we report cryo-EM structures of amyloid fibrils of wild-type human amylin and its S20G variant. The wild-type fibril structure, solved to 3.6-A resolution, contains two protofilaments, each built from S-shaped subunits. S20G fibrils, by contrast, contain two major polymorphs. Their structures, solved at 3.9-A and 4.0-A resolution, respectively, share a common two-protofilament core that is distinct from the wild-type structure. Remarkably, one polymorph contains a third subunit with another, distinct, cross-beta conformation. The presence of two different backbone conformations within the same fibril may explain the increased aggregation propensity of S20G, and illustrates a potential structural basis for surface-templated fibril assembly. | ||
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| + | Fibril structures of diabetes-related amylin variants reveal a basis for surface-templated assembly.,Gallardo R, Iadanza MG, Xu Y, Heath GR, Foster R, Radford SE, Ranson NA Nat Struct Mol Biol. 2020 Sep 14. pii: 10.1038/s41594-020-0496-3. doi:, 10.1038/s41594-020-0496-3. PMID:32929282<ref>PMID:32929282</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6zrf" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
amyloid structure of amylin (IAPP - islet amyloid polypeptide)
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