Atomic structure of the cross-[beta] spine of islet amyloid polypeptide (amylin)

Wiltzius, J J; Sievers, S A; Sawaya, M R; Cascio, D; Popov, D; Riekel, C; Eisenberg, D

doi:10.1110/ps.036509.108

Title: Atomic structure of the cross-[beta] spine of islet amyloid polypeptide (amylin)

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Abstract

Human islet amyloid polypeptide (IAPP or amylin) is a 37-residue hormone found as fibrillar deposits in pancreatic extracts of nearly all type II diabetics. Although the cellular toxicity of IAPP has been established, the structure of the fibrillar form found in these deposits is unknown. Here we have crystallized two segments from IAPP, which themselves form amyloid-like fibrils. The atomic structures of these two segments, NNFGAIL and SSTNVG, were determined, and form the basis of a model for the most commonly observed, full-length IAPP polymorph.

Authors:

Wiltzius, J J; Sievers, S A; Sawaya, M R; Cascio, D; Popov, D; Riekel, C; Eisenberg, D ^[1]

UCLA

Publication Date:: Fri Mar 27 00:00:00 EDT 2009

Research Org.:: Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)

Sponsoring Org.:: USDOE

OSTI Identifier:: 1007073

Resource Type:: Journal Article

Journal Name:: Protein Sci.

Additional Journal Information:: Journal Volume: 17; Journal Issue: (9) ; 09, 2008

Country of Publication:: United States

Language:: ENGLISH

Subject:: 59 BASIC BIOLOGICAL SCIENCES; 60 APPLIED LIFE SCIENCES; HUMAN POPULATIONS; HORMONES; POLYPEPTIDES; PANCREAS; DIABETES MELLITUS; MOLECULAR STRUCTURE

Citation Formats


                    Wiltzius, J J, Sievers, S A, Sawaya, M R, Cascio, D, Popov, D, Riekel, C, Eisenberg, D, and ESRF). Atomic structure of the cross-[beta] spine of islet amyloid polypeptide (amylin).  United States: N. p., 2009. 
        Web.  doi:10.1110/ps.036509.108.

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                    Wiltzius, J J, Sievers, S A, Sawaya, M R, Cascio, D, Popov, D, Riekel, C, Eisenberg, D, & ESRF). Atomic structure of the cross-[beta] spine of islet amyloid polypeptide (amylin).  United States.  https://doi.org/10.1110/ps.036509.108

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                    Wiltzius, J J, Sievers, S A, Sawaya, M R, Cascio, D, Popov, D, Riekel, C, Eisenberg, D, and ESRF). 2009.  
        "Atomic structure of the cross-[beta] spine of islet amyloid polypeptide (amylin)".  United States.  https://doi.org/10.1110/ps.036509.108.

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@article{osti_1007073,

  title        = {Atomic structure of the cross-[beta] spine of islet amyloid polypeptide (amylin)},

  author       = {Wiltzius, J J and Sievers, S A and Sawaya, M R and Cascio, D and Popov, D and Riekel, C and Eisenberg, D and ESRF)},

  abstractNote = {Human islet amyloid polypeptide (IAPP or amylin) is a 37-residue hormone found as fibrillar deposits in pancreatic extracts of nearly all type II diabetics. Although the cellular toxicity of IAPP has been established, the structure of the fibrillar form found in these deposits is unknown. Here we have crystallized two segments from IAPP, which themselves form amyloid-like fibrils. The atomic structures of these two segments, NNFGAIL and SSTNVG, were determined, and form the basis of a model for the most commonly observed, full-length IAPP polymorph.},

  doi          = {10.1110/ps.036509.108},

  url          = {https://www.osti.gov/biblio/1007073},
  journal      = {Protein Sci.},
number       = (9) ; 09, 2008,

  volume       = 17,

  place        = {United States},

  year         = {Fri Mar 27 00:00:00 EDT 2009},

  month        = {Fri Mar 27 00:00:00 EDT 2009}

}

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https://doi.org/10.1110/ps.036509.108

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