Molecular dynamics of the human RhD and RhAG blood group proteins
Introduction: Blood group antigens of the RH system (formerly known as “Rhesus”) play an important role in transfusion medicine because of the severe haemolytic consequences of antibodies to these antigens. No crystal structure is available for RhD proteins with its partner RhAG, and the precise sto...
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| Format: | Article |
| Language: | English |
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Frontiers Media S.A.
2024-03-01
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| Series: | Frontiers in Chemistry |
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| Online Access: | https://www.frontiersin.org/articles/10.3389/fchem.2024.1360392/full |
| _version_ | 1797257635358048256 |
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| author | Aline Floch Aline Floch Tatiana Galochkina France Pirenne France Pirenne Christophe Tournamille Christophe Tournamille Alexandre G. de Brevern |
| author_facet | Aline Floch Aline Floch Tatiana Galochkina France Pirenne France Pirenne Christophe Tournamille Christophe Tournamille Alexandre G. de Brevern |
| author_sort | Aline Floch |
| collection | DOAJ |
| description | Introduction: Blood group antigens of the RH system (formerly known as “Rhesus”) play an important role in transfusion medicine because of the severe haemolytic consequences of antibodies to these antigens. No crystal structure is available for RhD proteins with its partner RhAG, and the precise stoichiometry of the trimer complex remains unknown.Methods: To analyse their structural properties, the trimers formed by RhD and/or RhAG subunits were generated by protein modelling and molecular dynamics simulations were performed.Results: No major differences in structural behaviour were found between trimers of different compositions. The conformation of the subunits is relatively constant during molecular dynamics simulations, except for three large disordered loops.Discussion: This work makes it possible to propose a reasonable stoichiometry and demonstrates the potential of studying the structural behaviour of these proteins to investigate the hundreds of genetic variants relevant to transfusion medicine. |
| first_indexed | 2024-04-24T22:40:46Z |
| format | Article |
| id | doaj.art-b9e0b30885cd4f1c8b8bbe2513c226c1 |
| institution | Directory Open Access Journal |
| issn | 2296-2646 |
| language | English |
| last_indexed | 2024-04-24T22:40:46Z |
| publishDate | 2024-03-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| series | Frontiers in Chemistry |
| spelling | doaj.art-b9e0b30885cd4f1c8b8bbe2513c226c12024-03-19T04:44:58ZengFrontiers Media S.A.Frontiers in Chemistry2296-26462024-03-011210.3389/fchem.2024.13603921360392Molecular dynamics of the human RhD and RhAG blood group proteinsAline Floch0Aline Floch1Tatiana Galochkina2France Pirenne3France Pirenne4Christophe Tournamille5Christophe Tournamille6Alexandre G. de Brevern7University Paris Est Créteil, INSERM U955 Equipe Transfusion et Maladies du Globule Rouge, IMRB, Créteil, FranceLaboratoire de Biologie Médicale de Référence en Immuno-Hématologie Moléculaire, Etablissement Français du Sang Ile-de-France, Créteil, FranceUniversité Paris Cité and Université des Antilles and Université de la Réunion, Biologie Intégrée du Globule Rouge, UMR_S1134, BIGR, INSERM, DSIMB Bioinformatics team, Paris, FranceUniversity Paris Est Créteil, INSERM U955 Equipe Transfusion et Maladies du Globule Rouge, IMRB, Créteil, FranceLaboratoire de Biologie Médicale de Référence en Immuno-Hématologie Moléculaire, Etablissement Français du Sang Ile-de-France, Créteil, FranceUniversity Paris Est Créteil, INSERM U955 Equipe Transfusion et Maladies du Globule Rouge, IMRB, Créteil, FranceLaboratoire de Biologie Médicale de Référence en Immuno-Hématologie Moléculaire, Etablissement Français du Sang Ile-de-France, Créteil, FranceUniversité Paris Cité and Université des Antilles and Université de la Réunion, Biologie Intégrée du Globule Rouge, UMR_S1134, BIGR, INSERM, DSIMB Bioinformatics team, Paris, FranceIntroduction: Blood group antigens of the RH system (formerly known as “Rhesus”) play an important role in transfusion medicine because of the severe haemolytic consequences of antibodies to these antigens. No crystal structure is available for RhD proteins with its partner RhAG, and the precise stoichiometry of the trimer complex remains unknown.Methods: To analyse their structural properties, the trimers formed by RhD and/or RhAG subunits were generated by protein modelling and molecular dynamics simulations were performed.Results: No major differences in structural behaviour were found between trimers of different compositions. The conformation of the subunits is relatively constant during molecular dynamics simulations, except for three large disordered loops.Discussion: This work makes it possible to propose a reasonable stoichiometry and demonstrates the potential of studying the structural behaviour of these proteins to investigate the hundreds of genetic variants relevant to transfusion medicine.https://www.frontiersin.org/articles/10.3389/fchem.2024.1360392/fullRh blood group systemmembrane proteinsmolecular modelsmolecular dynamics simulationprotein structural elementsstructural alphabet |
| spellingShingle | Aline Floch Aline Floch Tatiana Galochkina France Pirenne France Pirenne Christophe Tournamille Christophe Tournamille Alexandre G. de Brevern Molecular dynamics of the human RhD and RhAG blood group proteins Frontiers in Chemistry Rh blood group system membrane proteins molecular models molecular dynamics simulation protein structural elements structural alphabet |
| title | Molecular dynamics of the human RhD and RhAG blood group proteins |
| title_full | Molecular dynamics of the human RhD and RhAG blood group proteins |
| title_fullStr | Molecular dynamics of the human RhD and RhAG blood group proteins |
| title_full_unstemmed | Molecular dynamics of the human RhD and RhAG blood group proteins |
| title_short | Molecular dynamics of the human RhD and RhAG blood group proteins |
| title_sort | molecular dynamics of the human rhd and rhag blood group proteins |
| topic | Rh blood group system membrane proteins molecular models molecular dynamics simulation protein structural elements structural alphabet |
| url | https://www.frontiersin.org/articles/10.3389/fchem.2024.1360392/full |
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