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5e5z
From Proteopedia
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==Structure of the amyloid forming peptide LVHSSN (residues== | ==Structure of the amyloid forming peptide LVHSSN (residues== | ||
| - | <StructureSection load='5e5z' size='340' side='right' caption='[[5e5z]], [[Resolution|resolution]] 1.66Å' scene=''> | + | <StructureSection load='5e5z' size='340' side='right'caption='[[5e5z]], [[Resolution|resolution]] 1.66Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5e5z]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5E5Z OCA]. For a <b>guided tour on the structure components</b> use [ | + | <table><tr><td colspan='2'>[[5e5z]] is a 1 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=5E5Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5E5Z FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.664Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5e5z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e5z OCA], [https://pdbe.org/5e5z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5e5z RCSB], [https://www.ebi.ac.uk/pdbsum/5e5z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5e5z ProSAT]</span></td></tr> |
</table> | </table> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Structural studies of amyloidogenic segments by X-ray crystallography have revealed a novel packing motif, consisting of out-of-register beta sheets, that may constitute one of the toxic species in aggregation related diseases. Here we sought to determine the presence of such a motif in Islet amyloid polypeptide (IAPP), whose amyloidogenic properties are associated with Type 2 Diabetes. We determined four new crystal structures of segments within IAPP all forming steric zippers. Most interestingly, one of the segments in the fibril core of IAPP forms an out-of-register steric zipper. Analysis of this structure reveals several commonalities with previously solved out-of-register fibrils. Our results provide evidence that out-of-register beta sheets may be a common structural motif in amyloid aggregates and may be associated with toxicity. | ||
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| - | Crystal Structures of IAPP Amyloidogenic Segments Reveal a Novel Packing Motif of Out-of-Register Beta Sheets.,Soriaga AB, Sangwan S, Macdonald R, Sawaya MR, Eisenberg D J Phys Chem B. 2015 Dec 2. PMID:26629790<ref>PMID:26629790</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 5e5z" style="background-color:#fffaf0;"></div> | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Homo sapiens]] |
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Eisenberg D]] |
| - | [[Category: | + | [[Category: Soriaga AB]] |
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Current revision
Structure of the amyloid forming peptide LVHSSN (residues
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