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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,
Language English Country United States
Document type Journal Article, Research Support, Non-U.S. Gov't
NLK
Free Medical Journals
from 1992 to 1 year ago
PubMed Central
from 1992 to 1 year ago
Europe PubMed Central
from 1992 to 1 year ago
Medline Complete (EBSCOhost)
from 2010-01-01 to 1 year ago
Wiley Free Content
from 1996 to 1 year ago
PubMed
31583778
DOI
10.1002/pro.3738
Knihovny.cz E-resources
- MeSH
- Acyl Coenzyme A chemistry metabolism MeSH
- Adaptor Proteins, Signal Transducing chemistry metabolism MeSH
- Humans MeSH
- Membrane Proteins chemistry metabolism MeSH
- Picornaviridae chemistry metabolism MeSH
- Binding Sites MeSH
- Check Tag
- Humans MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't 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.
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