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| | <StructureSection load='6zrr' size='340' side='right'caption='[[6zrr]], [[Resolution|resolution]] 4.00Å' scene=''> | | <StructureSection load='6zrr' size='340' side='right'caption='[[6zrr]], [[Resolution|resolution]] 4.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6zrr]] is a 18 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ZRR OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6ZRR FirstGlance]. <br> | + | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ZRR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6ZRR FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=TYC:L-TYROSINAMIDE'>TYC</scene></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]] 4Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6zrf|6zrf]], [[6zrq|6zrq]]</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'>[http://proteopedia.org/fgij/fg.htm?mol=6zrr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6zrr OCA], [http://pdbe.org/6zrr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6zrr RCSB], [http://www.ebi.ac.uk/pdbsum/6zrr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6zrr 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=6zrr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6zrr OCA], [https://pdbe.org/6zrr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6zrr RCSB], [https://www.ebi.ac.uk/pdbsum/6zrr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6zrr ProSAT]</span></td></tr> |
| | </table> | | </table> |
| - | == Function == | |
| - | [[http://www.uniprot.org/uniprot/IAPP_HUMAN IAPP_HUMAN]] Selectively inhibits insulin-stimulated glucose utilization and glycogen deposition in muscle, while not affecting adipocyte glucose metabolism. | |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Gallardo, R U]] | + | [[Category: Gallardo RU]] |
| - | [[Category: Iadanza, M G]] | + | [[Category: Iadanza MG]] |
| - | [[Category: Radford, S E]] | + | [[Category: Radford SE]] |
| - | [[Category: Ranson, N A]] | + | [[Category: Ranson NA]] |
| - | [[Category: Amyloid fibril type-2-diabetes early-onset]]
| + | |
| - | [[Category: Protein fibril]]
| + | |
| Structural highlights
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Gallardo R, Iadanza MG, Xu Y, Heath GR, Foster R, Radford SE, Ranson NA. Fibril structures of diabetes-related amylin variants reveal a basis for surface-templated assembly. Nat Struct Mol Biol. 2020 Sep 14. pii: 10.1038/s41594-020-0496-3. doi:, 10.1038/s41594-020-0496-3. PMID:32929282 doi:http://dx.doi.org/10.1038/s41594-020-0496-3
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