Nanomechanics of the MPMV Capsid-Protein-Binding RNA Fragment

Predicting Protein-Fragment Binding

Understanding the local structure surrounding the site of a protein-drug interaction can provide important insights into the mechanism of the drug and can help inform drug design and repurposing1. While structural information exists for a subset of protein-ligand interactions, it does not cover the space of all experimentally known interactions. As a result, the sites on proteins to which drugs...

Tethering in RNA: an RNA-binding fragment discovery tool.

Tethering has been extensively used to study small molecule interactions with proteins through reversible disulfide bond forming reactions to cysteine residues. We describe the adaptation of Tethering to the study of small molecule binding to RNA using a thiol-containing adenosine analog (ASH). Among 30 disulfide-containing small molecules screened for efficient Tethering to ASH-bearing RNAs de...

hev-capsid protein interacts with cytochrome p4502c8 and retinol-binding protein 4

Insertions within the hepatitis B virus capsid protein influence capsid formation and RNA encapsidation.

Hepatitis B virus (HBV) capsid proteins, termed core proteins, with two- to four-amino-acid insertions were assessed for capsid formation, RNA encapsidation, and the ability to support reverse transcription of the pregenome by the polymerase molecule. Velocity sedimentation analysis of insect cell-expressed recombinant core proteins revealed that only two of the nine insertion mutant proteins f...

Involvement of Vts1, a structure-specific RNA-binding protein, in Okazaki fragment processing in yeast

The non-essential VTS1 gene of Saccharomyces cerevisiae is highly conserved in eukaryotes and encodes a sequence- and structure-specific RNA-binding protein. The Vts1 protein has been implicated in post-transcriptional regulation of a specific set of mRNAs that contains its-binding site at their 3'-untranslated region. In this study, we identified VTS1 as a multi-copy suppressor of dna2-K1080E,...