Structural and strategic landscape of PIKK protein family and their inhibitors: an overview
| Autor: | Deekshi Angira, Althaf Shaik, Vijay Thiruvenkatam |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2020 |
| Předmět: |
pikk
phosphatidylinositol-3 kinase-related kinases mtor mammalian target of rapamycin atr atm- and rad3-related kinase atm ataxia telangiectasia mutated kinase dna-pkcs dna dependent protein catalytic subunit trrap transformation-transactivation domain-associated protein hsmg1 suppressor with morphological effect on genitalia family member dna damage response Biochemistry QD415-436 Biology (General) QH301-705.5 |
| Zdroj: | Frontiers in Bioscience-Landmark, Vol 25, Iss 8, Pp 1538-1567 (2020) |
| Druh dokumentu: | article |
| ISSN: | 2768-6701 |
| DOI: | 10.2741/4867 |
| Popis: | Phosphatidylinositol-3 kinase-related kinases (PIKKs) is a class of six unique serine/threonine kinases that are characterized as high molecular mass colossal proteins present in multicellular organisms. They predominantly regulate the innumerable eukaryotic cellular processes, for instance, cell-signaling cascades related to DNA damage and repair, cell growth and proliferation, cell cycle arrest, genome surveillance, gene expression and many other important yet diverse functions. A characteristic PIKK member comprises of an N-terminal HEAT domain, followed by FAT domain, a highly conserved kinase catalytic domain, and a C-terminal FATC domain. In this comprehensive review, we reassess and discuss various established functions of all the six PIKK members with each function corroborated by their structural topology. In addition to the domain architecture of these atypical kinases, their specific inhibitors have been briefly deliberated. This review gives us the impression of the emergent importance of PIKKs, which, despite of their complexity, are the hub of research with respect to the inhibitor development. |
| Databáze: | Directory of Open Access Journals |
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