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-Structure paper
| タイトル | The Arthropoda-specific Tramtrack group BTB protein domains use previously unknown interface to form hexamers. |
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| ジャーナル・号・ページ | Elife, Vol. 13, Year 2024 |
| 掲載日 | 2024年9月2日 |
著者 | Artem N Bonchuk / Konstantin I Balagurov / Rozbeh Baradaran / Konstantin M Boyko / Nikolai N Sluchanko / Anastasia M Khrustaleva / Anna D Burtseva / Olga V Arkova / Karina K Khalisova / Vladimir O Popov / Andreas Naschberger / Pavel G Georgiev / ![]() |
| PubMed 要旨 | BTB (bric-a-brack, Tramtrack, and broad complex) is a diverse group of protein-protein interaction domains found within metazoan proteins. Transcription factors contain a dimerizing BTB subtype with ...BTB (bric-a-brack, Tramtrack, and broad complex) is a diverse group of protein-protein interaction domains found within metazoan proteins. Transcription factors contain a dimerizing BTB subtype with a characteristic N-terminal extension. The Tramtrack group (TTK) is a distinct type of BTB domain, which can multimerize. Single-particle cryo-EM microscopy revealed that the TTK-type BTB domains assemble into a hexameric structure consisting of three canonical BTB dimers connected through a previously uncharacterized interface. We demonstrated that the TTK-type BTB domains are found only in Arthropods and have undergone lineage-specific expansion in modern insects. The genome encodes 24 transcription factors with TTK-type BTB domains, whereas only four have non-TTK-type BTB domains. Yeast two-hybrid analysis revealed that the TTK-type BTB domains have an unusually broad potential for heteromeric associations presumably through a dimer-dimer interaction interface. Thus, the TTK-type BTB domains are a structurally and functionally distinct group of protein domains specific to Arthropodan transcription factors. |
リンク | Elife / PubMed:39221775 / PubMed Central |
| 手法 | EM (単粒子) |
| 解像度 | 3.3 Å |
| 構造データ | EMDB-19049, PDB-8rc6: |
| 由来 |
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キーワード | TRANSCRIPTION / DNA-binding / transcription regulation / oligomerization |
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