Importance of Coiled-Coil Motif in Human Cytomegalovirus Protein UL77
Author Information
Author(s): Christina Meissner, Sylvia Köppen-Rung, Pánja Dittmer, Alexandra Lapp, Sara Bogner, Elke Bogner
Primary Institution: Institute of Virology, Charité Universitätsmedizin Berlin, Berlin, Germany
Hypothesis
The study investigates the role of the coiled-coil motif in the oligomerization and DNA binding properties of the human cytomegalovirus protein UL77.
Conclusion
The coiled-coil motif in pUL77 is crucial for its oligomerization and ability to bind double-stranded DNA.
Supporting Evidence
- pUL77 can form homodimers and is crucial for DNA binding.
- The coiled-coil motif is necessary for the oligomerization of pUL77.
- pUL77 interacts with capsid-associated DNA packaging proteins.
Takeaway
The protein UL77 from the human cytomegalovirus needs a special part called a coiled-coil motif to stick together and grab onto DNA.
Methodology
The study used immunoprecipitation, in vitro binding assays, and co-immunoprecipitation to analyze the interactions and functions of pUL77.
Digital Object Identifier (DOI)
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