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Structural insights into Acyl-coenzyme A binding domain containing 3 (ACBD3) protein hijacking by picornaviruses
D. Chalupska, B. Różycki, M. Klima, E. Boura,
Jazyk angličtina Země Spojené státy americké
Typ dokumentu časopisecké články, práce podpořená grantem
NLK
Free Medical Journals
od 1992 do Před 1 rokem
PubMed Central
od 1992 do Před 1 rokem
Europe PubMed Central
od 1992 do Před 1 rokem
Medline Complete (EBSCOhost)
od 2010-01-01 do Před 1 rokem
Wiley Free Content
od 1996 do Před 1 rokem
PubMed
31583778
DOI
10.1002/pro.3738
Knihovny.cz E-zdroje
- MeSH
- acylkoenzym A chemie metabolismus MeSH
- adaptorové proteiny signální transdukční chemie metabolismus MeSH
- lidé MeSH
- membránové proteiny chemie metabolismus MeSH
- Picornaviridae chemie metabolismus MeSH
- vazebná místa MeSH
- Check Tag
- lidé MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
Many picornaviruses hijack the Golgi resident Acyl-coenzyme A binding domain containing 3 (ACBD3) protein in order to recruit the phosphatidylinositol 4-kinase B (PI4KB) to viral replication organelles (ROs). PI4KB, once recruited and activated by ACBD3 protein, produces the lipid phosphatidylinositol 4-phosphate (PI4P), which is a key step in the biogenesis of viral ROs. To do so, picornaviruses use their small nonstructural protein 3A that binds the Golgi dynamics domain of the ACBD3 protein. Here, we present the analysis of the highly flexible ACBD3 proteins and the viral 3A protein in solution using small-angle X-ray scattering and computer simulations. Our analysis revealed that both the ACBD3 protein and the 3A:ACBD3 protein complex have an extended and flexible conformation in solution.
Citace poskytuje Crossref.org
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