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The zipper groups of the amyloid state of proteins
Fibrous proteins in the amyloid state are found both associated with numerous diseases and in the normal functions of cells. Amyloid fibers contain a repetitive spine, commonly built from a pair of β-sheets whose β-strands run perpendicular to the fiber direction and whose side chains interdigitate,...
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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International Union of Crystallography
2013
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3606035/ https://www.ncbi.nlm.nih.gov/pubmed/23519662 http://dx.doi.org/10.1107/S0907444912050548 |
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author | Stroud, James C. |
author_facet | Stroud, James C. |
author_sort | Stroud, James C. |
collection | PubMed |
description | Fibrous proteins in the amyloid state are found both associated with numerous diseases and in the normal functions of cells. Amyloid fibers contain a repetitive spine, commonly built from a pair of β-sheets whose β-strands run perpendicular to the fiber direction and whose side chains interdigitate, much like the teeth of a zipper. In fiber spines known as homosteric zippers, identical protein segments sharing identical packing environments make the two β-sheets. In previous work based on atomic resolution crystal structures of homosteric zippers derived from a dozen proteins, the symmetries of homosteric zippers were categorized into eight classes. Here, it is shown through a formal derivation that each homosteric zipper class corresponds to a unique set of symmetry groups termed ‘zipper groups’. Furthermore, the eight previously identified classes do not account for all of the 15 possible zipper groups, which may be categorized into the complete set of ten classes. Because of their foundations in group theory, the 15 zipper groups provide a mathematically rigorous classification for homosteric zippers. |
format | Online Article Text |
id | pubmed-3606035 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | International Union of Crystallography |
record_format | MEDLINE/PubMed |
spelling | pubmed-36060352013-05-10 The zipper groups of the amyloid state of proteins Stroud, James C. Acta Crystallogr D Biol Crystallogr Research Papers Fibrous proteins in the amyloid state are found both associated with numerous diseases and in the normal functions of cells. Amyloid fibers contain a repetitive spine, commonly built from a pair of β-sheets whose β-strands run perpendicular to the fiber direction and whose side chains interdigitate, much like the teeth of a zipper. In fiber spines known as homosteric zippers, identical protein segments sharing identical packing environments make the two β-sheets. In previous work based on atomic resolution crystal structures of homosteric zippers derived from a dozen proteins, the symmetries of homosteric zippers were categorized into eight classes. Here, it is shown through a formal derivation that each homosteric zipper class corresponds to a unique set of symmetry groups termed ‘zipper groups’. Furthermore, the eight previously identified classes do not account for all of the 15 possible zipper groups, which may be categorized into the complete set of ten classes. Because of their foundations in group theory, the 15 zipper groups provide a mathematically rigorous classification for homosteric zippers. International Union of Crystallography 2013-03-09 /pmc/articles/PMC3606035/ /pubmed/23519662 http://dx.doi.org/10.1107/S0907444912050548 Text en © Stroud 2013 http://creativecommons.org/licenses/by/2.0/uk/ This is an open-access article distributed under the terms of the Creative Commons Attribution Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited. |
spellingShingle | Research Papers Stroud, James C. The zipper groups of the amyloid state of proteins |
title | The zipper groups of the amyloid state of proteins |
title_full | The zipper groups of the amyloid state of proteins |
title_fullStr | The zipper groups of the amyloid state of proteins |
title_full_unstemmed | The zipper groups of the amyloid state of proteins |
title_short | The zipper groups of the amyloid state of proteins |
title_sort | zipper groups of the amyloid state of proteins |
topic | Research Papers |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3606035/ https://www.ncbi.nlm.nih.gov/pubmed/23519662 http://dx.doi.org/10.1107/S0907444912050548 |
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