6y1a: Difference between revisions
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==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 == | |||
<table><tr><td colspan='2'>[[6y1a]] is a 16 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. 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 [https://proteopedia.org/fgij/fg.htm?mol=6Y1A FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4.2Å</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'>[https://proteopedia.org/fgij/fg.htm?mol=6y1a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6y1a OCA], [https://pdbe.org/6y1a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6y1a RCSB], [https://www.ebi.ac.uk/pdbsum/6y1a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6y1a ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6y1a" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</SX> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Gremer L]] | |||
[[Category: Hoyer W]] | |||
[[Category: Kupreichyk T]] | |||
[[Category: Pothula KR]] | |||
[[Category: Ravelli RBG]] | |||
[[Category: Roeder C]] | |||
[[Category: Schaefer LU]] | |||
[[Category: Schroder GF]] | |||
[[Category: Willbold D]] | |||
