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NeProc predicts binding segments in intrinsically disordered regions without learning binding region sequences

Intrinsically disordered proteins are those proteins with intrinsically disordered regions. One of the unique characteristics of intrinsically disordered proteins is the existence of functional segments in intrinsically dis­ordered regions. These segments are involved in binding to partner molecules...

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Detalles Bibliográficos
Autores principales: Anbo, Hiroto, Amagai, Hiroki, Fukuchi, Satoshi
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Biophysical Society of Japan 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7692026/
https://www.ncbi.nlm.nih.gov/pubmed/33304713
http://dx.doi.org/10.2142/biophysico.BSJ-2020026
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author Anbo, Hiroto
Amagai, Hiroki
Fukuchi, Satoshi
author_facet Anbo, Hiroto
Amagai, Hiroki
Fukuchi, Satoshi
author_sort Anbo, Hiroto
collection PubMed
description Intrinsically disordered proteins are those proteins with intrinsically disordered regions. One of the unique characteristics of intrinsically disordered proteins is the existence of functional segments in intrinsically dis­ordered regions. These segments are involved in binding to partner molecules, such as protein and DNA, and play important roles in signaling pathways and/or transcriptional regulation. Although there are databases that gather information on such disordered binding regions, data remain limited. Therefore, it is desirable to develop programs to predict the disordered binding regions without using data for the binding regions. We developed a program, NeProc, to predict the disordered binding regions, which can be regarded as intrinsically disordered regions with a structural propensity. We only used data for the structural domains and intrinsically disordered regions to detect such regions. NeProc accepts a query amino acid sequence converted into a position specific score matrix, and uses two neural networks that employ different window sizes, a neural network of short windows, and a neural network of long windows. The performance of NeProc was comparable to that of existing programs of the disordered binding region prediction. This result presents the possibility to overcome the shortage of the disordered binding region data in the development of the prediction programs for these binding regions. NeProc is available at http://flab.neproc.org/neproc/index.html
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spelling pubmed-76920262020-12-09 NeProc predicts binding segments in intrinsically disordered regions without learning binding region sequences Anbo, Hiroto Amagai, Hiroki Fukuchi, Satoshi Biophys Physicobiol Database and Computer Program Intrinsically disordered proteins are those proteins with intrinsically disordered regions. One of the unique characteristics of intrinsically disordered proteins is the existence of functional segments in intrinsically dis­ordered regions. These segments are involved in binding to partner molecules, such as protein and DNA, and play important roles in signaling pathways and/or transcriptional regulation. Although there are databases that gather information on such disordered binding regions, data remain limited. Therefore, it is desirable to develop programs to predict the disordered binding regions without using data for the binding regions. We developed a program, NeProc, to predict the disordered binding regions, which can be regarded as intrinsically disordered regions with a structural propensity. We only used data for the structural domains and intrinsically disordered regions to detect such regions. NeProc accepts a query amino acid sequence converted into a position specific score matrix, and uses two neural networks that employ different window sizes, a neural network of short windows, and a neural network of long windows. The performance of NeProc was comparable to that of existing programs of the disordered binding region prediction. This result presents the possibility to overcome the shortage of the disordered binding region data in the development of the prediction programs for these binding regions. NeProc is available at http://flab.neproc.org/neproc/index.html The Biophysical Society of Japan 2020-11-03 /pmc/articles/PMC7692026/ /pubmed/33304713 http://dx.doi.org/10.2142/biophysico.BSJ-2020026 Text en 2020 THE BIOPHYSICAL SOCIETY OF JAPAN https://creativecommons.org/licenses/by-nc-sa/4.0/This article is licensed under the Creative Commons Attribution-NonCommercial-ShareAlike 4.0 Inter­national License. To view a copy of this license, visit 
https://creativecommons.org/licenses/by-nc-sa/4.0/.
spellingShingle Database and Computer Program
Anbo, Hiroto
Amagai, Hiroki
Fukuchi, Satoshi
NeProc predicts binding segments in intrinsically disordered regions without learning binding region sequences
title NeProc predicts binding segments in intrinsically disordered regions without learning binding region sequences
title_full NeProc predicts binding segments in intrinsically disordered regions without learning binding region sequences
title_fullStr NeProc predicts binding segments in intrinsically disordered regions without learning binding region sequences
title_full_unstemmed NeProc predicts binding segments in intrinsically disordered regions without learning binding region sequences
title_short NeProc predicts binding segments in intrinsically disordered regions without learning binding region sequences
title_sort neproc predicts binding segments in intrinsically disordered regions without learning binding region sequences
topic Database and Computer Program
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7692026/
https://www.ncbi.nlm.nih.gov/pubmed/33304713
http://dx.doi.org/10.2142/biophysico.BSJ-2020026
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