Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Single-stranded-RNA binding proteins.

A A Antson1

  • 1York Structural Biology Laboratory, Department of Chemistry, University of York, York, YO10 5DD, UK. fred@yorvic.york.ac.uk

Current Opinion in Structural Biology
|February 19, 2000
PubMed
Summary
This summary is machine-generated.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

[Contraction of the disordered loop located within C-terminal domain of the transcriptional regulator HlyIIR causes its structural rearrangement].

Molekuliarnaia biologiia·2009
Same author

Structure of the human S100A12-copper complex: implications for host-parasite defence.

Acta crystallographica. Section D, Biological crystallography·2003
Same author

The structure of S100A12 in a hexameric form and its proposed role in receptor signalling.

Acta crystallographica. Section D, Biological crystallography·2002
Same author

Understanding the mechanism of ice binding by type III antifreeze proteins.

Journal of molecular biology·2001
Same author

The three-dimensional structure of human S100A12.

Acta crystallographica. Section D, Biological crystallography·2001
Same author

Structure of the intact transactivation domain of the human papillomavirus E2 protein.

Nature·2000
Same journal

Tomogram exploration through template matching and deep learning.

Current opinion in structural biology·2026
Same journal

A comparative review of cryo-electron ptychography: Biological applications and future perspectives.

Current opinion in structural biology·2026
Same journal

Metabolic disruptions through a three-dimensional genomic lens.

Current opinion in structural biology·2026
Same journal

Collective variable design for biomolecular conformational dynamics.

Current opinion in structural biology·2026
Same journal

Polymer scaling in protein crowding: From dilute coils to semidilute meshes.

Current opinion in structural biology·2026
Same journal

Tuning the physicochemical properties of rationally designed protein-based biomolecular condensates.

Current opinion in structural biology·2026
See all related articles

Structural studies reveal how proteins bind to single-stranded RNA, showing unique backbone conformations beyond classical double helix models. This advances understanding of RNA-protein interactions.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Protein-RNA interactions are crucial in biological processes.
  • Knowledge was limited for interactions with single-stranded RNA (ssRNA).
  • Previous studies focused on structured RNA molecules.

Purpose of the Study:

  • To elucidate the structural basis of protein interactions with single-stranded RNA.
  • To understand how proteins accommodate and bind to unfolded RNA segments.

Main Methods:

  • Determination of crystal structures of protein complexes.
  • Analysis of four structures involving extended single-stranded RNA molecules.

Main Results:

  • Revealed specific patterns of protein binding to RNA bases.

Related Experiment Videos

  • Demonstrated that the RNA sugar-phosphate backbone adopts non-classical conformations.
  • Showcased protein adaptability to accommodate ssRNA.

    • Conclusions:

    • Protein interactions with ssRNA are structurally well-defined.
    • These interactions involve unique backbone conformations distinct from double helices.
    • The findings provide key insights into RNA recognition by proteins.