5ko0

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<StructureSection load='5ko0' size='340' side='right'caption='[[5ko0]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
<StructureSection load='5ko0' size='340' side='right'caption='[[5ko0]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5ko0]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KO0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5KO0 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5ko0]] is a 2 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=5KO0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5KO0 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SCN:THIOCYANATE+ION'>SCN</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron crystallography, [[Resolution|Resolution]] 1.4&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[5knz|5knz]]</div></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SCN:THIOCYANATE+ION'>SCN</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=5ko0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ko0 OCA], [https://pdbe.org/5ko0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ko0 RCSB], [https://www.ebi.ac.uk/pdbsum/5ko0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ko0 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=5ko0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ko0 OCA], [https://pdbe.org/5ko0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ko0 RCSB], [https://www.ebi.ac.uk/pdbsum/5ko0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ko0 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[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.
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[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.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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hIAPP fibrils are associated with Type-II Diabetes, but the link of hIAPP structure to islet cell death remains elusive. Here we observe that hIAPP fibrils are cytotoxic to cultured pancreatic beta-cells, leading us to determine the structure and cytotoxicity of protein segments composing the amyloid spine of hIAPP. Using the cryoEM method MicroED, we discover that one segment, 19-29 S20G, forms pairs of beta-sheets mated by a dry interface that share structural features with and are similarly cytotoxic to full-length hIAPP fibrils. In contrast, a second segment, 15-25 WT, forms non-toxic labile beta-sheets. These segments possess different structures and cytotoxic effects, however, both can seed full-length hIAPP, and cause hIAPP to take on the cytotoxic and structural features of that segment. These results suggest that protein segment structures represent polymorphs of their parent protein and that segment 19-29 S20G may serve as a model for the toxic spine of hIAPP.
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Atomic structures of fibrillar segments of hIAPP suggest tightly mated beta-sheets are important for cytotoxicity.,Krotee P, Rodriguez JA, Sawaya MR, Cascio D, Reyes FE, Shi D, Hattne J, Nannenga BL, Oskarsson ME, Philipp S, Griner S, Jiang L, Glabe CG, Westermark GT, Gonen T, Eisenberg DS Elife. 2017 Jan 3;6. doi: 10.7554/eLife.19273. PMID:28045370<ref>PMID:28045370</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5ko0" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Cascio, D]]
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[[Category: Cascio D]]
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[[Category: Eisenberg, D S]]
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[[Category: Eisenberg DS]]
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[[Category: Gonen, T]]
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[[Category: Gonen T]]
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[[Category: Hattne, J]]
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[[Category: Hattne J]]
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[[Category: Krotee, P A.L]]
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[[Category: Krotee PAL]]
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[[Category: Nannenga, B L]]
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[[Category: Nannenga BL]]
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[[Category: Reyes, F E]]
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[[Category: Reyes FE]]
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[[Category: Rodriguez, J A]]
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[[Category: Rodriguez JA]]
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[[Category: Sawaya, M R]]
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[[Category: Sawaya MR]]
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[[Category: Shi, D]]
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[[Category: Shi D]]
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[[Category: Amyloid]]
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[[Category: Islet amyloid polypeptide]]
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[[Category: Microed]]
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[[Category: Protein fibril]]
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[[Category: Toxic spine]]
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[[Category: Type ii diabetes]]
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Current revision

Human Islet Amyloid Polypeptide Segment 15-FLVHSSNNFGA-25 Determined by MicroED

PDB ID 5ko0

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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