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6zrq
From Proteopedia
(Difference between revisions)
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==two-protofilament amyloid structure of S20G variant of human amylin (IAPP - islet amyloid polypeptide)== | ==two-protofilament amyloid structure of S20G variant of human amylin (IAPP - islet amyloid polypeptide)== | ||
| - | <StructureSection load='6zrq' size='340' side='right'caption='[[6zrq]]' scene=''> | + | <StructureSection load='6zrq' size='340' side='right'caption='[[6zrq]], [[Resolution|resolution]] 3.90Å' 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=6ZRQ OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6ZRQ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6zrq]] is a 12 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ZRQ OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6ZRQ FirstGlance]. <br> |
| - | </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=6zrq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6zrq OCA], [http://pdbe.org/6zrq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6zrq RCSB], [http://www.ebi.ac.uk/pdbsum/6zrq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6zrq ProSAT]</span></td></tr> | + | </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> |
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6zrf|6zrf]]</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=6zrq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6zrq OCA], [http://pdbe.org/6zrq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6zrq RCSB], [http://www.ebi.ac.uk/pdbsum/6zrq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6zrq 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;"> | ||
| + | == 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<ref>PMID:32929282</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6zrq" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Gallardo | + | [[Category: Gallardo, R U]] |
| - | [[Category: Iadanza | + | [[Category: Iadanza, M G]] |
| - | [[Category: Radford | + | [[Category: Radford, S E]] |
| - | [[Category: Ranson | + | [[Category: Ranson, N A]] |
| + | [[Category: Amyloid fibril type-2-diabetes early-onset]] | ||
| + | [[Category: Protein fibril]] | ||
Current revision
two-protofilament amyloid structure of S20G variant of human amylin (IAPP - islet amyloid polypeptide)
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