1kuw

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[[Image:1kuw.jpg|left|200px]]
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{{Seed}}
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[[Image:1kuw.png|left|200px]]
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{{STRUCTURE_1kuw| PDB=1kuw | SCENE= }}
{{STRUCTURE_1kuw| PDB=1kuw | SCENE= }}
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'''High-Resolution Structure and Localization of Amylin Nucleation Site in Detergent Micelles'''
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===High-Resolution Structure and Localization of Amylin Nucleation Site in Detergent Micelles===
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==Overview==
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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.
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The line below this paragraph, {{ABSTRACT_PUBMED_12717720}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 12717720 is the PubMed ID number.
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{{ABSTRACT_PUBMED_12717720}}
==About this Structure==
==About this Structure==
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1KUW is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KUW OCA].
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1KUW is a [[Single protein]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KUW OCA].
==Reference==
==Reference==
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[[Category: Orientation]]
[[Category: Orientation]]
[[Category: Solution nmr]]
[[Category: Solution nmr]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 23:11:40 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 11:02:41 2008''

Revision as of 08:02, 2 July 2008

Image:1kuw.png

Template:STRUCTURE 1kuw

High-Resolution Structure and Localization of Amylin Nucleation Site in Detergent Micelles

Template:ABSTRACT PUBMED 12717720

About this Structure

1KUW is a Single protein structure. Full experimental information is available from OCA.

Reference

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

Page seeded by OCA on Wed Jul 2 11:02:41 2008

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