6vw2: Difference between revisions

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<StructureSection load='6vw2' size='340' side='right'caption='[[6vw2]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
<StructureSection load='6vw2' size='340' side='right'caption='[[6vw2]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6vw2]] is a 10 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6VW2 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6VW2 FirstGlance]. <br>
<table><tr><td colspan='2'>[[6vw2]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6VW2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6VW2 FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">IAPP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.4&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6vw2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vw2 OCA], [http://pdbe.org/6vw2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6vw2 RCSB], [http://www.ebi.ac.uk/pdbsum/6vw2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6vw2 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=6vw2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vw2 OCA], [https://pdbe.org/6vw2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6vw2 RCSB], [https://www.ebi.ac.uk/pdbsum/6vw2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6vw2 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/SMT3_YEAST SMT3_YEAST]] Not known; suppressor of MIF2 mutations.
[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.[https://www.uniprot.org/uniprot/SMT3_YEAST SMT3_YEAST] Not known; suppressor of MIF2 mutations.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Human islet amyloid polypeptide (hIAPP) functions as a glucose-regulating hormone but deposits as amyloid fibrils in more than 90% of patients with type II diabetes (T2D). Here we report the cryo-EM structure of recombinant full-length hIAPP fibrils. The fibril is composed of two symmetrically related protofilaments with ordered residues 14-37. Our hIAPP fibril structure (i) supports the previous hypothesis that residues 20-29 constitute the core of the hIAPP amyloid; (ii) suggests a molecular mechanism for the action of the hIAPP hereditary mutation S20G; (iii) explains why the six residue substitutions in rodent IAPP prevent aggregation; and (iv) suggests regions responsible for the observed hIAPP cross-seeding with beta-amyloid. Furthermore, we performed structure-based inhibitor design to generate potential hIAPP aggregation inhibitors. Four of the designed peptides delay hIAPP aggregation in vitro, providing a starting point for the development of T2D therapeutics and proof of concept that the capping strategy can be used on full-length cryo-EM fibril structures.
 
Cryo-EM structure and inhibitor design of human IAPP (amylin) fibrils.,Cao Q, Boyer DR, Sawaya MR, Ge P, Eisenberg DS Nat Struct Mol Biol. 2020 Jun 15. pii: 10.1038/s41594-020-0435-3. doi:, 10.1038/s41594-020-0435-3. PMID:32541896<ref>PMID:32541896</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6vw2" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Boyer, D R]]
[[Category: Saccharomyces cerevisiae S288C]]
[[Category: Cao, Q]]
[[Category: Boyer DR]]
[[Category: Eisenberg, D S]]
[[Category: Cao Q]]
[[Category: Sawaya, M R]]
[[Category: Eisenberg DS]]
[[Category: Amyloid]]
[[Category: Sawaya MR]]
[[Category: Hiapp]]
[[Category: Protein fibril]]
[[Category: Type ii diabetes]]

Latest revision as of 14:40, 6 March 2024

Cryo-EM structure of human islet amyloid polypeptide (hIAPP, or amylin) fibrils

6vw2, resolution 3.40Å

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