A5018688727- Viral Infections and Outbreaks Research
- Bacillus and Francisella bacterial research
- RNA Research and Splicing
- Hepatitis B Virus Studies
- RNA and protein synthesis mechanisms
- Influenza Virus Research Studies
- SARS-CoV-2 and COVID-19 Research
- Viral Infections and Immunology Research
- DNA and Nucleic Acid Chemistry
- Bacteriophages and microbial interactions
- RNA regulation and disease
- RNA Interference and Gene Delivery
- Viral Infections and Vectors
- Neonatal Respiratory Health Research
- Genomics and Chromatin Dynamics
Washington University in St. Louis
2020-2024
Rice University
2018
Abstract Protein-protein and protein-nucleic acid interactions are often considered difficult drug targets because the surfaces involved lack obvious druggable pockets. Cryptic pockets could present opportunities for targeting these interactions, but identifying exploiting remains challenging. Here, we apply a general pipeline cryptic to interferon inhibitory domain (IID) of Ebola virus viral protein 35 (VP35). VP35 plays multiple essential roles in Ebola’s replication cycle lacks that...
Cryptic pockets are of growing interest as potential drug targets, particularly to control protein-nucleic acid interactions that often occur via flat surfaces. However, it remains unclear whether cryptic contribute protein function or if they merely happenstantial features can easily be evolved away achieve resistance. Here, we explore a pocket in the Interferon Inhibitory Domain (IID) viral 35 (VP35) Zaire ebolavirus aids its ability bind double-stranded RNA (dsRNA). We use simulations and...
Cryptic pockets are of growing interest as potential drug targets, particularly to control protein-nucleic acid interactions that often occur via flat surfaces. However, it remains unclear whether cryptic contribute protein function or if they merely happenstantial features can easily be evolved away achieve resistance. Here, we explore a pocket in the Interferon Inhibitory Domain (IID) viral 35 (VP35) Zaire ebolavirus aids its ability bind double-stranded RNA (dsRNA). We use simulations and...
Abstract Protein-protein and protein-nucleic acid interactions are often considered difficult drug targets because the surfaces involved lack obvious druggable pockets. Cryptic pockets could present opportunities for targeting these interactions, but identifying exploiting remains challenging. Here, we apply a general pipeline cryptic to interferon inhibitory domain (IID) of Ebola viral protein 35 (VP35). VP35 plays multiple essential roles in Ebola’s replication cycle lacks that utility...
The short 8-10 amino acid "hinge" sequence in lactose repressor (LacI), present other LacI/GalR family members, links DNA and inducer-binding domains. Structural studies of full-length or truncated LacI-operator complexes demonstrate insertion the dimeric helical structure at center operator sequence. This association bends ∼40° aligns flanking semi-symmetric sites for optimal contact by N-terminal helix-turn-helix (HtH) sequences within each dimer. In contrast, hinge region remains unfolded...
Abstract Cryptic pockets are of growing interest as potential drug targets, particularly to control protein-nucleic acid interactions that often occur via flat surfaces. However, it remains unclear whether cryptic contribute protein function or if they merely happenstantial features can easily be evolved away achieve resistance. Here, we explore a pocket in the Interferon Inhibitory Domain (IID) viral 35 (VP35) Zaire ebolavirus aids its ability bind double-stranded RNA (dsRNA). We use...