Abstract
Recently, progress has been made towards the structural characterization of the novel folds of RNA-bound arginine-rich peptides and the architecture of their peptide-binding RNA pockets in viral and phage systems. These studies are based on an approach whereby the peptide and RNA components are minimalist modular domains that undergo adaptive structural transitions upon complex formation. Such complexes are characterized by recognition alignments in which the tertiary fold of the RNA generates binding pockets with the potential to envelop minimal elements of protein secondary structure. Strikingly, the peptides fold as isolated α-helical or β-hairpin folds within their RNA major-groove targets, without the necessity of additional appendages for anchorage within the binding pocket. The RNA peptide-binding pocket architectures are sculptured through precisely positioned mismatches, triples and looped-out bases, which accommodate amino acid sidechains through hydrophobic, hydrogen bonding and ionic intermolecular contacts. By contrast, protein modules associated with the HIV-1 nucleocapsid and MS2 phage coat target their RNA binding sites through the insertion of specificity-determining RNA base residues within conserved hydrophobic pockets and crevices on the protein surface, with the bases anchored through hydrogen bonding interactions. These alternative strategies of RNA recognition at the peptide and protein module level provide novel insights into the principles, patterns and diversity of the adaptive transitions associated with the recognition process.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.