Searching for New Z-DNA/Z-RNA Binding Proteins Based on Structural Similarity to Experimentally Validated Z alpha Domain

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F68081707%3A_____%2F22%3A00555058" target="_blank" >RIV/68081707:_____/22:00555058 - isvavai.cz</a>
Result on the web
<a href="https://www.mdpi.com/1422-0067/23/2/768" target="_blank" >https://www.mdpi.com/1422-0067/23/2/768</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.3390/ijms23020768" target="_blank" >10.3390/ijms23020768</a>

Result language
angličtina
Original language name
Searching for New Z-DNA/Z-RNA Binding Proteins Based on Structural Similarity to Experimentally Validated Z alpha Domain
Original language description
Z-DNA and Z-RNA are functionally important left-handed structures of nucleic acids, which play a significant role in several molecular and biological processes including DNA replication, gene expression regulation and viral nucleic acid sensing. Most proteins that have been proven to interact with Z-DNA/Z-RNA contain the so-called Z alpha domain, which is structurally well conserved. To date, only eight proteins with Z alpha domain have been described within a few organisms (including human, mouse, Danio rerio, Trypanosoma brucei and some viruses). Therefore, this paper aimed to search for new Z-DNA/Z-RNA binding proteins in the complete PDB structures database and from the AlphaFold2 protein models. A structure-based similarity search found 14 proteins with highly similar Z alpha domain structure in experimentally-defined proteins and 185 proteins with a putative Z alpha domain using the AlphaFold2 models. Structure-based alignment and molecular docking confirmed high functional conservation of amino acids involved in Z-DNA/Z-RNA, suggesting that Z-DNA/Z-RNA recognition may play an important role in a variety of cellular processes.
Czech name
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Czech description
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Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10608 - Biochemistry and molecular biology

Project
<a href="/en/project/GA22-21903S" target="_blank" >GA22-21903S: Local DNA structures and their role in mutant p53 protein function in human tumours</a><br>
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year
2022
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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