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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...

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Autores principales: Bashir, Samirul, Pal, Debnath, Qadri, Ozaira, Banday, Mariam, Fazili, Khalid
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
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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.
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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
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AT paldebnath quaternarystructureanalysisofire1
AT qadriozaira quaternarystructureanalysisofire1
AT bandaymariam quaternarystructureanalysisofire1
AT fazilikhalid quaternarystructureanalysisofire1