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Membranome 3.0: Database of single‐pass membrane proteins with AlphaFold models
The Membranome database provides comprehensive structural information on single‐pass (i.e., bitopic) membrane proteins from six evolutionarily distant organisms, including protein–protein interactions, complexes, mutations, experimental structures, and models of transmembrane α‐helical dimers. We pr...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
John Wiley & Sons, Inc.
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9047035/ https://www.ncbi.nlm.nih.gov/pubmed/35481632 http://dx.doi.org/10.1002/pro.4318 |
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author | Lomize, Andrei L. Schnitzer, Kevin A. Todd, Spencer C. Cherepanov, Stanislav Outeiral, Carlos Deane, Charlotte M. Pogozheva, Irina D. |
author_facet | Lomize, Andrei L. Schnitzer, Kevin A. Todd, Spencer C. Cherepanov, Stanislav Outeiral, Carlos Deane, Charlotte M. Pogozheva, Irina D. |
author_sort | Lomize, Andrei L. |
collection | PubMed |
description | The Membranome database provides comprehensive structural information on single‐pass (i.e., bitopic) membrane proteins from six evolutionarily distant organisms, including protein–protein interactions, complexes, mutations, experimental structures, and models of transmembrane α‐helical dimers. We present a new version of this database, Membranome 3.0, which was significantly updated by revising the set of 5,758 bitopic proteins and incorporating models generated by AlphaFold 2 in the database. The AlphaFold models were parsed into structural domains located at the different membrane sides, modified to exclude low‐confidence unstructured terminal regions and signal sequences, validated through comparison with available experimental structures, and positioned with respect to membrane boundaries. Membranome 3.0 was re‐developed to facilitate visualization and comparative analysis of multiple 3D structures of proteins that belong to a specified family, complex, biological pathway, or membrane type. New tools for advanced search and analysis of proteins, their interactions, complexes, and mutations were included. The database is freely accessible at https://membranome.org. |
format | Online Article Text |
id | pubmed-9047035 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | John Wiley & Sons, Inc. |
record_format | MEDLINE/PubMed |
spelling | pubmed-90470352022-05-02 Membranome 3.0: Database of single‐pass membrane proteins with AlphaFold models Lomize, Andrei L. Schnitzer, Kevin A. Todd, Spencer C. Cherepanov, Stanislav Outeiral, Carlos Deane, Charlotte M. Pogozheva, Irina D. Protein Sci Tools for Protein Science The Membranome database provides comprehensive structural information on single‐pass (i.e., bitopic) membrane proteins from six evolutionarily distant organisms, including protein–protein interactions, complexes, mutations, experimental structures, and models of transmembrane α‐helical dimers. We present a new version of this database, Membranome 3.0, which was significantly updated by revising the set of 5,758 bitopic proteins and incorporating models generated by AlphaFold 2 in the database. The AlphaFold models were parsed into structural domains located at the different membrane sides, modified to exclude low‐confidence unstructured terminal regions and signal sequences, validated through comparison with available experimental structures, and positioned with respect to membrane boundaries. Membranome 3.0 was re‐developed to facilitate visualization and comparative analysis of multiple 3D structures of proteins that belong to a specified family, complex, biological pathway, or membrane type. New tools for advanced search and analysis of proteins, their interactions, complexes, and mutations were included. The database is freely accessible at https://membranome.org. John Wiley & Sons, Inc. 2022-04-28 2022-05 /pmc/articles/PMC9047035/ /pubmed/35481632 http://dx.doi.org/10.1002/pro.4318 Text en © 2022 The Authors. Protein Science published by Wiley Periodicals LLC on behalf of The Protein Society. https://creativecommons.org/licenses/by/4.0/This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Tools for Protein Science Lomize, Andrei L. Schnitzer, Kevin A. Todd, Spencer C. Cherepanov, Stanislav Outeiral, Carlos Deane, Charlotte M. Pogozheva, Irina D. Membranome 3.0: Database of single‐pass membrane proteins with AlphaFold models |
title | Membranome 3.0: Database of single‐pass membrane proteins with AlphaFold models |
title_full | Membranome 3.0: Database of single‐pass membrane proteins with AlphaFold models |
title_fullStr | Membranome 3.0: Database of single‐pass membrane proteins with AlphaFold models |
title_full_unstemmed | Membranome 3.0: Database of single‐pass membrane proteins with AlphaFold models |
title_short | Membranome 3.0: Database of single‐pass membrane proteins with AlphaFold models |
title_sort | membranome 3.0: database of single‐pass membrane proteins with alphafold models |
topic | Tools for Protein Science |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9047035/ https://www.ncbi.nlm.nih.gov/pubmed/35481632 http://dx.doi.org/10.1002/pro.4318 |
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