Cargando…
Quaternary structure analysis of IRE1
IRE1 belongs to a type I transmembrane protein family harboring two functional domains, cytoplasmic domain with kinase and RNAse catalytic activity, and the luminal domain, which is involved in the sensing of unfolded proteins. IRE1 molecule undergoes dimerization in the lumenal domain, which functi...
Autores principales: | , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Caltech Library
2023
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10091119/ https://www.ncbi.nlm.nih.gov/pubmed/37065768 http://dx.doi.org/10.17912/micropub.biology.000763 |
_version_ | 1785023087448686592 |
---|---|
author | Bashir, Samirul Pal, Debnath Qadri, Ozaira Banday, Mariam Fazili, Khalid |
author_facet | Bashir, Samirul Pal, Debnath Qadri, Ozaira Banday, Mariam Fazili, Khalid |
author_sort | Bashir, Samirul |
collection | PubMed |
description | IRE1 belongs to a type I transmembrane protein family harboring two functional domains, cytoplasmic domain with kinase and RNAse catalytic activity, and the luminal domain, which is involved in the sensing of unfolded proteins. IRE1 molecule undergoes dimerization in the lumenal domain, which functionally activates the catalytic C-terminal domain. IRE1 activation is directly related to transition between monomeric and dimeric forms. We have deduced two quaternary structures from the published crystal structure of IRE1. One structure with a large stable interface that requires large activation and deactivation energy to active IRE1. The other quaternary structure has low dissociation energy and is more suitable for IRE1 oligomeric transition. |
format | Online Article Text |
id | pubmed-10091119 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | Caltech Library |
record_format | MEDLINE/PubMed |
spelling | pubmed-100911192023-04-13 Quaternary structure analysis of IRE1 Bashir, Samirul Pal, Debnath Qadri, Ozaira Banday, Mariam Fazili, Khalid MicroPubl Biol New Finding IRE1 belongs to a type I transmembrane protein family harboring two functional domains, cytoplasmic domain with kinase and RNAse catalytic activity, and the luminal domain, which is involved in the sensing of unfolded proteins. IRE1 molecule undergoes dimerization in the lumenal domain, which functionally activates the catalytic C-terminal domain. IRE1 activation is directly related to transition between monomeric and dimeric forms. We have deduced two quaternary structures from the published crystal structure of IRE1. One structure with a large stable interface that requires large activation and deactivation energy to active IRE1. The other quaternary structure has low dissociation energy and is more suitable for IRE1 oligomeric transition. Caltech Library 2023-03-28 /pmc/articles/PMC10091119/ /pubmed/37065768 http://dx.doi.org/10.17912/micropub.biology.000763 Text en Copyright: © 2023 by the authors https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. |
spellingShingle | New Finding Bashir, Samirul Pal, Debnath Qadri, Ozaira Banday, Mariam Fazili, Khalid Quaternary structure analysis of IRE1 |
title | Quaternary structure analysis of IRE1 |
title_full | Quaternary structure analysis of IRE1 |
title_fullStr | Quaternary structure analysis of IRE1 |
title_full_unstemmed | Quaternary structure analysis of IRE1 |
title_short | Quaternary structure analysis of IRE1 |
title_sort | quaternary structure analysis of ire1 |
topic | New Finding |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10091119/ https://www.ncbi.nlm.nih.gov/pubmed/37065768 http://dx.doi.org/10.17912/micropub.biology.000763 |
work_keys_str_mv | AT bashirsamirul quaternarystructureanalysisofire1 AT paldebnath quaternarystructureanalysisofire1 AT qadriozaira quaternarystructureanalysisofire1 AT bandaymariam quaternarystructureanalysisofire1 AT fazilikhalid quaternarystructureanalysisofire1 |