Constructing networks for comparison of collagen types

Collagens are structural proteins that are predominantly found in the extracellular matrix of multicellular animals, where they are mainly responsible for the stability and structural integrity of various tissues. All collagens contain polypeptide strands (α-chains). There are several types of colla...

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Main Authors: Wesp Valentin, Scholz Lukas, Ziermann-Canabarro Janine M., Schuster Stefan, Stark Heiko
Format: Article
Language:English
Published: De Gruyter 2024-07-01
Series:Journal of Integrative Bioinformatics
Subjects:
Online Access:https://doi.org/10.1515/jib-2024-0020
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author Wesp Valentin
Scholz Lukas
Ziermann-Canabarro Janine M.
Schuster Stefan
Stark Heiko
author_facet Wesp Valentin
Scholz Lukas
Ziermann-Canabarro Janine M.
Schuster Stefan
Stark Heiko
author_sort Wesp Valentin
collection DOAJ
description Collagens are structural proteins that are predominantly found in the extracellular matrix of multicellular animals, where they are mainly responsible for the stability and structural integrity of various tissues. All collagens contain polypeptide strands (α-chains). There are several types of collagens, some of which differ significantly in form, function, and tissue specificity. Because of their importance in clinical research, they are grouped into subdivisions, the so-called collagen families, and their sequences are often analysed. However, problems arise with highly homologous sequence segments. To increase the accuracy of collagen classification and prediction of their functions, the structure of these collagens and their expression in different tissues could result in a better focus on sequence segments of interest. Here, we analyse collagen families with different levels of conservation. As a result, clusters with high interconnectivity can be found, such as the fibrillar collagens, the COL4 network-forming collagens, and the COL9 FACITs. Furthermore, a large cluster between network-forming, FACIT, and COL28a1 α-chains is formed with COL6a3 as a major hub node. The formation of clusters also signifies, why it is important to always analyse the α-chains and why structural changes can have a wide range of effects on the body.
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series Journal of Integrative Bioinformatics
spelling doaj-art-b926ba0f65ef4acea3e37237a89fd7c02024-12-02T12:04:10ZengDe GruyterJournal of Integrative Bioinformatics1613-45162024-07-0121321110.1515/jib-2024-0020Constructing networks for comparison of collagen typesWesp Valentin0Scholz Lukas1Ziermann-Canabarro Janine M.2Schuster Stefan3Stark Heiko4Department of Bioinformatics, 64341Friedrich-Schiller-University Jena, Jena, GermanyDepartment of Bioinformatics, 64341Friedrich-Schiller-University Jena, Jena, GermanyDepartment of Anatomy, Howard University College of Medicine, Washington, DC, USADepartment of Bioinformatics, 64341Friedrich-Schiller-University Jena, Jena, GermanyDepartment of Bioinformatics, 64341Friedrich-Schiller-University Jena, Jena, GermanyCollagens are structural proteins that are predominantly found in the extracellular matrix of multicellular animals, where they are mainly responsible for the stability and structural integrity of various tissues. All collagens contain polypeptide strands (α-chains). There are several types of collagens, some of which differ significantly in form, function, and tissue specificity. Because of their importance in clinical research, they are grouped into subdivisions, the so-called collagen families, and their sequences are often analysed. However, problems arise with highly homologous sequence segments. To increase the accuracy of collagen classification and prediction of their functions, the structure of these collagens and their expression in different tissues could result in a better focus on sequence segments of interest. Here, we analyse collagen families with different levels of conservation. As a result, clusters with high interconnectivity can be found, such as the fibrillar collagens, the COL4 network-forming collagens, and the COL9 FACITs. Furthermore, a large cluster between network-forming, FACIT, and COL28a1 α-chains is formed with COL6a3 as a major hub node. The formation of clusters also signifies, why it is important to always analyse the α-chains and why structural changes can have a wide range of effects on the body.https://doi.org/10.1515/jib-2024-0020α-chainsalphafoldcollagenhigh-confidence regionnetwork analysis
spellingShingle Wesp Valentin
Scholz Lukas
Ziermann-Canabarro Janine M.
Schuster Stefan
Stark Heiko
Constructing networks for comparison of collagen types
Journal of Integrative Bioinformatics
α-chains
alphafold
collagen
high-confidence region
network analysis
title Constructing networks for comparison of collagen types
title_full Constructing networks for comparison of collagen types
title_fullStr Constructing networks for comparison of collagen types
title_full_unstemmed Constructing networks for comparison of collagen types
title_short Constructing networks for comparison of collagen types
title_sort constructing networks for comparison of collagen types
topic α-chains
alphafold
collagen
high-confidence region
network analysis
url https://doi.org/10.1515/jib-2024-0020
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AT ziermanncanabarrojaninem constructingnetworksforcomparisonofcollagentypes
AT schusterstefan constructingnetworksforcomparisonofcollagentypes
AT starkheiko constructingnetworksforcomparisonofcollagentypes