Modelling of C-terminal tail of human STING and its interaction with tank-binding kinase 1

dc.contributor.authorEşsiz, Şebnem
dc.contributor.authorAudu-Bida, Hajara
dc.contributor.authorEssiz, Sebnem
dc.date.accessioned2023-10-19T15:12:53Z
dc.date.available2023-10-19T15:12:53Z
dc.date.issued2022
dc.department-temp[Ata Ouda Al-Masri, Rahaf; Audu-Bida, Hajara; Essiz, Sebnem] Kadir Has Univ, Fac Engn & Nat Sci, Dept Mol Biol & Genet, Istanbul, Turkeyen_US
dc.description.abstractStimulator of interferon genes (STING) plays a significant role in a cell's intracellular defense against pathogens or self DNA by inducing inflammation or apoptosis through a pathway known as cGAS-cGAMP-STING. STING uses one of its domains, the C-terminal tail (CTT) to recruit the members of the pathway. However, the structure of this domain has not been solved experimentally. STING conformation is open and more flexible when inactive. When STING gets activated by cGAMP, its conformation changes to a closed state covered by 4 beta-sheets over the binding site. This conformational change leads to its binding to Tank-binding kinase 1 (TBK1). TBK1 then phosphorylates STING aiding its entry to the cell's nucleus. In this study, we focused on the loop modeling of the CTT domain in both the active and inactive STING conformations. After the modeling step, the active and inactive STING structures were docked to one of the cGAS-cGAMP-STING pathway members, TBK1, to observe the differences of binding modes. CTT loop stayed higher in the active structure, while all the best-scored models, active or inactive, ended up around the same position with respect to TBK1. However, when the STING poses are compared with the cryo-EM image of the complex structure, the models in the active structure chain B displayed closer results to the complex structure.en_US
dc.identifier.citation0
dc.identifier.doi10.3906/biy-2108-90en_US
dc.identifier.endpage81en_US
dc.identifier.issn1300-0152
dc.identifier.issn1303-6092
dc.identifier.issue1en_US
dc.identifier.pmid37533668en_US
dc.identifier.scopus2-s2.0-85125440579en_US
dc.identifier.scopusqualityQ2
dc.identifier.startpage69en_US
dc.identifier.trdizinidhttps://search.trdizin.gov.tr/yayin/detay/521621en_US
dc.identifier.urihttps://doi.org/10.3906/biy-2108-90
dc.identifier.uri521621
dc.identifier.urihttps://hdl.handle.net/20.500.12469/5556
dc.identifier.volume46en_US
dc.identifier.wosWOS:000753542100002en_US
dc.identifier.wosqualityQ3
dc.khas20231019-WoSen_US
dc.language.isoenen_US
dc.publisherTubitak Scientific & Technical Research Council Turkeyen_US
dc.relation.ispartofTurkish Journal of Biologyen_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/openAccessen_US
dc.subjectLoop modelingen_US
dc.subjectcGAS-cGAMP-STING pathwayen_US
dc.subjectstimulator of interferon genes (STING)en_US
dc.subjectTank-binding kinase 1 (TBK1)en_US
dc.subjectC-terminal tail (CTT) domainen_US
dc.subjectprotein-protein dockingen_US
dc.titleModelling of C-terminal tail of human STING and its interaction with tank-binding kinase 1en_US
dc.typeArticleen_US
dspace.entity.typePublication
relation.isAuthorOfPublicationa83da4e2-c934-413a-886f-2438d0a3fd58
relation.isAuthorOfPublication.latestForDiscoverya83da4e2-c934-413a-886f-2438d0a3fd58

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