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6y1a
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==Amyloid fibril structure of islet amyloid polypeptide== | ==Amyloid fibril structure of islet amyloid polypeptide== | ||
| - | < | + | <SX load='6y1a' size='340' side='right' viewer='molstar' caption='[[6y1a]], [[Resolution|resolution]] 4.20Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[6y1a]] is a 16 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6Y1A OCA]. For a <b>guided tour on the structure components</b> use [http:// | + | <table><tr><td colspan='2'>[[6y1a]] is a 16 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6Y1A OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6Y1A FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http:// | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6y1a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6y1a OCA], [http://pdbe.org/6y1a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6y1a RCSB], [http://www.ebi.ac.uk/pdbsum/6y1a PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6y1a ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == 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. | [[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 == | ||
| + | Amyloid deposits consisting of fibrillar islet amyloid polypeptide (IAPP) in pancreatic islets are associated with beta-cell loss and have been implicated in type 2 diabetes (T2D). Here, we applied cryo-EM to reconstruct densities of three dominant IAPP fibril polymorphs, formed in vitro from synthetic human IAPP. An atomic model of the main polymorph, built from a density map of 4.2-A resolution, reveals two S-shaped, intertwined protofilaments. The segment 21-NNFGAIL-27, essential for IAPP amyloidogenicity, forms the protofilament interface together with Tyr37 and the amidated C terminus. The S-fold resembles polymorphs of Alzheimer's disease (AD)-associated amyloid-beta (Abeta) fibrils, which might account for the epidemiological link between T2D and AD and reports on IAPP-Abeta cross-seeding in vivo. The results structurally link the early-onset T2D IAPP genetic polymorphism (encoding Ser20Gly) with the AD Arctic mutation (Glu22Gly) of Abeta and support the design of inhibitors and imaging probes for IAPP fibrils. | ||
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| + | Cryo-EM structure of islet amyloid polypeptide fibrils reveals similarities with amyloid-beta fibrils.,Roder C, Kupreichyk T, Gremer L, Schafer LU, Pothula KR, Ravelli RBG, Willbold D, Hoyer W, Schroder GF Nat Struct Mol Biol. 2020 Jul;27(7):660-667. doi: 10.1038/s41594-020-0442-4. Epub, 2020 Jun 15. PMID:32541895<ref>PMID:32541895</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6y1a" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
| - | </ | + | </SX> |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Gremer, L]] | [[Category: Gremer, L]] | ||
Current revision
Amyloid fibril structure of islet amyloid polypeptide
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Categories: Large Structures | Gremer, L | Hoyer, W | Kupreichyk, T | Pothula, K R | Ravelli, R B.G | Roeder, C | Schaefer, L U | Schroder, G F | Willbold, D | Amylin | Amyloid fibril | Diabetes | Hormone | Iapp
