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Spatial Structure of Lectin from the Mussel Mytilus trossulus: In-Sights from Molecular Modelling and Practical Proof

Most proteins have the ability to self-associate into homooligomeric protein complexes, which consist of two or more identical subunits. Today, modern methods of molecular modeling are an integral part of the study of many biologically active molecules. In silico methods are widely used in structure...

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Autores principales: Filshtein, Alina P., Chikalovets, Irina V., Mizgina, Tatyana O., Lukyanov, Pavel A., Hua, Kuo-Feng, Chernikov, Oleg V.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9866010/
https://www.ncbi.nlm.nih.gov/pubmed/36662183
http://dx.doi.org/10.3390/md21010010
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author Filshtein, Alina P.
Chikalovets, Irina V.
Mizgina, Tatyana O.
Lukyanov, Pavel A.
Hua, Kuo-Feng
Chernikov, Oleg V.
author_facet Filshtein, Alina P.
Chikalovets, Irina V.
Mizgina, Tatyana O.
Lukyanov, Pavel A.
Hua, Kuo-Feng
Chernikov, Oleg V.
author_sort Filshtein, Alina P.
collection PubMed
description Most proteins have the ability to self-associate into homooligomeric protein complexes, which consist of two or more identical subunits. Today, modern methods of molecular modeling are an integral part of the study of many biologically active molecules. In silico methods are widely used in structure establishing and function and activity prediction of lectins – carbohydrate-binding proteins. Here, we described by computer simulation the spatial organization of lectin isolated from the mantle of the mussel Mytilus trossulus (MTL). It was shown that the dimerization of MTL gives a total of six ligand binding sites that may be important for the manifestation its biological properties. The ability of MTL to form a dimeric and oligomeric structure was confirmed by dynamic light scattering and SDS-PAGE methods.
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spelling pubmed-98660102023-01-22 Spatial Structure of Lectin from the Mussel Mytilus trossulus: In-Sights from Molecular Modelling and Practical Proof Filshtein, Alina P. Chikalovets, Irina V. Mizgina, Tatyana O. Lukyanov, Pavel A. Hua, Kuo-Feng Chernikov, Oleg V. Mar Drugs Communication Most proteins have the ability to self-associate into homooligomeric protein complexes, which consist of two or more identical subunits. Today, modern methods of molecular modeling are an integral part of the study of many biologically active molecules. In silico methods are widely used in structure establishing and function and activity prediction of lectins – carbohydrate-binding proteins. Here, we described by computer simulation the spatial organization of lectin isolated from the mantle of the mussel Mytilus trossulus (MTL). It was shown that the dimerization of MTL gives a total of six ligand binding sites that may be important for the manifestation its biological properties. The ability of MTL to form a dimeric and oligomeric structure was confirmed by dynamic light scattering and SDS-PAGE methods. MDPI 2022-12-23 /pmc/articles/PMC9866010/ /pubmed/36662183 http://dx.doi.org/10.3390/md21010010 Text en © 2022 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Communication
Filshtein, Alina P.
Chikalovets, Irina V.
Mizgina, Tatyana O.
Lukyanov, Pavel A.
Hua, Kuo-Feng
Chernikov, Oleg V.
Spatial Structure of Lectin from the Mussel Mytilus trossulus: In-Sights from Molecular Modelling and Practical Proof
title Spatial Structure of Lectin from the Mussel Mytilus trossulus: In-Sights from Molecular Modelling and Practical Proof
title_full Spatial Structure of Lectin from the Mussel Mytilus trossulus: In-Sights from Molecular Modelling and Practical Proof
title_fullStr Spatial Structure of Lectin from the Mussel Mytilus trossulus: In-Sights from Molecular Modelling and Practical Proof
title_full_unstemmed Spatial Structure of Lectin from the Mussel Mytilus trossulus: In-Sights from Molecular Modelling and Practical Proof
title_short Spatial Structure of Lectin from the Mussel Mytilus trossulus: In-Sights from Molecular Modelling and Practical Proof
title_sort spatial structure of lectin from the mussel mytilus trossulus: in-sights from molecular modelling and practical proof
topic Communication
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9866010/
https://www.ncbi.nlm.nih.gov/pubmed/36662183
http://dx.doi.org/10.3390/md21010010
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