3dgj: Difference between revisions

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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3dgj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dgj OCA], [https://pdbe.org/3dgj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3dgj RCSB], [https://www.ebi.ac.uk/pdbsum/3dgj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3dgj 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=3dgj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dgj OCA], [https://pdbe.org/3dgj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3dgj RCSB], [https://www.ebi.ac.uk/pdbsum/3dgj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3dgj ProSAT]</span></td></tr>
</table>
</table>
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== Publication Abstract from PubMed ==
Human Islet Amyloid Polypeptide (IAPP or amylin) is a 37-residue hormone found as fibrillar deposits in pancreatic extracts of nearly all type II diabetics. Although the cellular toxicity of IAPP has been established, the structure of the fibrillar form found in these deposits is unknown. Here we have crystallized two segments from IAPP, which themselves form amyloid-like fibrils. The atomic structures of these two segments, NNFGAIL and SSTNVG were determined and form the basis of a model for the most commonly observed, full-length IAPP polymorph.
Atomic structure of the cross-{beta} spine of Islet Amyloid Polypeptide (Amylin).,Wiltzius JJ, Sievers SA, Sawaya MR, Cascio D, Popov D, Riekel C, Eisenberg D Protein Sci. 2008 Jun 12;. PMID:18556473<ref>PMID:18556473</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3dgj" style="background-color:#fffaf0;"></div>
== References ==
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