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Physical Motif Clustering within Intrinsically Disordered Nucleoporin Sequences Reveals Universal Functional Features
Bioinformatics of disordered proteins is especially challenging given high mutation rates for homologous proteins and that functionality may not be strongly related to sequence. Here we have performed a novel bioinformatic analysis, based on the spatial clustering of physically relevant features suc...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2013
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3774778/ https://www.ncbi.nlm.nih.gov/pubmed/24066078 http://dx.doi.org/10.1371/journal.pone.0073831 |
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author | Ando, David Colvin, Michael Rexach, Michael Gopinathan, Ajay |
author_facet | Ando, David Colvin, Michael Rexach, Michael Gopinathan, Ajay |
author_sort | Ando, David |
collection | PubMed |
description | Bioinformatics of disordered proteins is especially challenging given high mutation rates for homologous proteins and that functionality may not be strongly related to sequence. Here we have performed a novel bioinformatic analysis, based on the spatial clustering of physically relevant features such as binding motifs and charges within disordered proteins, on thousands of Nuclear Pore Complex (NPC) FG motif containing proteins (FG nups). The biophysical mechanism by which FG nups regulate nucleocytoplasmic transport has remained elusive. Our analysis revealed a set of highly conserved spatial features in the sequence structure of individual FG nups, such as the separation, localization, and ordering of FG motifs and charged residues along the protein chain. These functionally conserved features provide insight into the particular biophysical mechanisms responsible for regulation of nucleocytoplasmic traffic in the NPC, strongly constraining current models. Additionally this method allows us to identify potentially functionally analogous disordered proteins across distantly related species. |
format | Online Article Text |
id | pubmed-3774778 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-37747782013-09-24 Physical Motif Clustering within Intrinsically Disordered Nucleoporin Sequences Reveals Universal Functional Features Ando, David Colvin, Michael Rexach, Michael Gopinathan, Ajay PLoS One Research Article Bioinformatics of disordered proteins is especially challenging given high mutation rates for homologous proteins and that functionality may not be strongly related to sequence. Here we have performed a novel bioinformatic analysis, based on the spatial clustering of physically relevant features such as binding motifs and charges within disordered proteins, on thousands of Nuclear Pore Complex (NPC) FG motif containing proteins (FG nups). The biophysical mechanism by which FG nups regulate nucleocytoplasmic transport has remained elusive. Our analysis revealed a set of highly conserved spatial features in the sequence structure of individual FG nups, such as the separation, localization, and ordering of FG motifs and charged residues along the protein chain. These functionally conserved features provide insight into the particular biophysical mechanisms responsible for regulation of nucleocytoplasmic traffic in the NPC, strongly constraining current models. Additionally this method allows us to identify potentially functionally analogous disordered proteins across distantly related species. Public Library of Science 2013-09-16 /pmc/articles/PMC3774778/ /pubmed/24066078 http://dx.doi.org/10.1371/journal.pone.0073831 Text en © 2013 Ando et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited. |
spellingShingle | Research Article Ando, David Colvin, Michael Rexach, Michael Gopinathan, Ajay Physical Motif Clustering within Intrinsically Disordered Nucleoporin Sequences Reveals Universal Functional Features |
title | Physical Motif Clustering within Intrinsically Disordered Nucleoporin Sequences Reveals Universal Functional Features |
title_full | Physical Motif Clustering within Intrinsically Disordered Nucleoporin Sequences Reveals Universal Functional Features |
title_fullStr | Physical Motif Clustering within Intrinsically Disordered Nucleoporin Sequences Reveals Universal Functional Features |
title_full_unstemmed | Physical Motif Clustering within Intrinsically Disordered Nucleoporin Sequences Reveals Universal Functional Features |
title_short | Physical Motif Clustering within Intrinsically Disordered Nucleoporin Sequences Reveals Universal Functional Features |
title_sort | physical motif clustering within intrinsically disordered nucleoporin sequences reveals universal functional features |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3774778/ https://www.ncbi.nlm.nih.gov/pubmed/24066078 http://dx.doi.org/10.1371/journal.pone.0073831 |
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