View source for 1kuw


==High-Resolution Structure and Localization of Amylin Nucleation Site in Detergent Micelles==
<StructureSection load='1kuw' size='340' side='right'caption='[[1kuw]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1kuw]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KUW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KUW FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1kuw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kuw OCA], [https://pdbe.org/1kuw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kuw RCSB], [https://www.ebi.ac.uk/pdbsum/1kuw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kuw 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.
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== Publication Abstract from PubMed ==
Human islet amyloid polypeptide (hIAPP), or amylin, is a 37 amino acid hormone secreted by pancreatic beta-cells. hIAPP constitutes approximately 90% of the amyloid deposits found in type II diabetic patients. It has been shown that the central region of the peptide (hIAPP(20-29)) constitutes the nucleation site for the amyloidogenic process with F23 playing a key role in the formation of the beta-pleated structures. In addition, it has been proposed that an important stage in the cytotoxicity of hIAPP is its interaction with the beta-cell membranes. As a first step toward the characterization of the interaction of hIAPP with cell membranes, we determined conformational preferences of hIAPP(20-29) in membrane-mimicking environments. We found that upon interacting with negatively charged micelles, the dominant conformation of hIAPP(20-29) is a distorted type I beta-turn centered on residues F23 and G24, with F23, A25, and I26 forming a small hydrophobic cluster that may facilitate the interaction of this peptide with the membrane bilayer. Moreover, we were able to elucidate the topological orientation of the peptide that is absorbed on the micelle surface, with the hydrophobic cluster oriented toward the hydrocarbon region of the micelles and both N- and C-termini exposed to the solvent.

Conformational preferences of the amylin nucleation site in SDS micelles: an NMR study.,Mascioni A, Porcelli F, Ilangovan U, Ramamoorthy A, Veglia G Biopolymers. 2003 May;69(1):29-41. PMID:12717720<ref>PMID:12717720</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1kuw" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Ilangovan U]]
[[Category: Mascioni A]]
[[Category: Porcelli F]]
[[Category: Ramamoorthy A]]
[[Category: Veglia G]]