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Recognizing ion ligand binding sites by SMO algorithm

BACKGROUND: In many important life activities, the execution of protein function depends on the interaction between proteins and ligands. As an important protein binding ligand, the identification of the binding site of the ion ligands plays an important role in the study of the protein function. RE...

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Autores principales: Wang, Shan, Hu, Xiuzhen, Feng, Zhenxing, Zhang, Xiaojin, Liu, Liu, Sun, Kai, Xu, Shuang
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BioMed Central 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6905020/
https://www.ncbi.nlm.nih.gov/pubmed/31823742
http://dx.doi.org/10.1186/s12860-019-0237-9
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author Wang, Shan
Hu, Xiuzhen
Feng, Zhenxing
Zhang, Xiaojin
Liu, Liu
Sun, Kai
Xu, Shuang
author_facet Wang, Shan
Hu, Xiuzhen
Feng, Zhenxing
Zhang, Xiaojin
Liu, Liu
Sun, Kai
Xu, Shuang
author_sort Wang, Shan
collection PubMed
description BACKGROUND: In many important life activities, the execution of protein function depends on the interaction between proteins and ligands. As an important protein binding ligand, the identification of the binding site of the ion ligands plays an important role in the study of the protein function. RESULTS: In this study, four acid radical ion ligands (NO(2)(−),CO(3)(2−),SO(4)(2−),PO(4)(3−)) and ten metal ion ligands (Zn(2+),Cu(2+),Fe(2+),Fe(3+),Ca(2+),Mg(2+),Mn(2+),Na(+),K(+),Co(2+)) are selected as the research object, and the Sequential minimal optimization (SMO) algorithm based on sequence information was proposed, better prediction results were obtained by 5-fold cross validation. CONCLUSIONS: An efficient method for predicting ion ligand binding sites was presented.
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spelling pubmed-69050202019-12-30 Recognizing ion ligand binding sites by SMO algorithm Wang, Shan Hu, Xiuzhen Feng, Zhenxing Zhang, Xiaojin Liu, Liu Sun, Kai Xu, Shuang BMC Mol Cell Biol Research BACKGROUND: In many important life activities, the execution of protein function depends on the interaction between proteins and ligands. As an important protein binding ligand, the identification of the binding site of the ion ligands plays an important role in the study of the protein function. RESULTS: In this study, four acid radical ion ligands (NO(2)(−),CO(3)(2−),SO(4)(2−),PO(4)(3−)) and ten metal ion ligands (Zn(2+),Cu(2+),Fe(2+),Fe(3+),Ca(2+),Mg(2+),Mn(2+),Na(+),K(+),Co(2+)) are selected as the research object, and the Sequential minimal optimization (SMO) algorithm based on sequence information was proposed, better prediction results were obtained by 5-fold cross validation. CONCLUSIONS: An efficient method for predicting ion ligand binding sites was presented. BioMed Central 2019-12-11 /pmc/articles/PMC6905020/ /pubmed/31823742 http://dx.doi.org/10.1186/s12860-019-0237-9 Text en © The Author(s). 2019 Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.
spellingShingle Research
Wang, Shan
Hu, Xiuzhen
Feng, Zhenxing
Zhang, Xiaojin
Liu, Liu
Sun, Kai
Xu, Shuang
Recognizing ion ligand binding sites by SMO algorithm
title Recognizing ion ligand binding sites by SMO algorithm
title_full Recognizing ion ligand binding sites by SMO algorithm
title_fullStr Recognizing ion ligand binding sites by SMO algorithm
title_full_unstemmed Recognizing ion ligand binding sites by SMO algorithm
title_short Recognizing ion ligand binding sites by SMO algorithm
title_sort recognizing ion ligand binding sites by smo algorithm
topic Research
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6905020/
https://www.ncbi.nlm.nih.gov/pubmed/31823742
http://dx.doi.org/10.1186/s12860-019-0237-9
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