Unknown

Dataset Information

0

Protein-RNA interactions: structural biology and computational modeling techniques.


ABSTRACT: RNA-binding proteins are functionally diverse within cells, being involved in RNA-metabolism, translation, DNA damage repair, and gene regulation at both the transcriptional and post-transcriptional levels. Much has been learnt about their interactions with RNAs through structure determination techniques and computational modeling. This review gives an overview of the structural data currently available for protein-RNA complexes, and discusses the technical issues facing structural biologists working to solve their structures. The review focuses on three techniques used to solve the 3-dimensional structure of protein-RNA complexes at atomic resolution, namely X-ray crystallography, solution nuclear magnetic resonance (NMR) and cryo-electron microscopy (cryo-EM). The review then focuses on the main computational modeling techniques that use these atomic resolution data: discussing the prediction of RNA-binding sites on unbound proteins, docking proteins, and RNAs, and modeling the molecular dynamics of the systems. In conclusion, the review looks at the future directions this field of research might take.

SUBMITTER: Jones S 

PROVIDER: S-EPMC5430296 | biostudies-literature | 2016 Dec

REPOSITORIES: biostudies-literature

altmetric image

Publications

Protein-RNA interactions: structural biology and computational modeling techniques.

Jones Susan S  

Biophysical reviews 20161114 4


RNA-binding proteins are functionally diverse within cells, being involved in RNA-metabolism, translation, DNA damage repair, and gene regulation at both the transcriptional and post-transcriptional levels. Much has been learnt about their interactions with RNAs through structure determination techniques and computational modeling. This review gives an overview of the structural data currently available for protein-RNA complexes, and discusses the technical issues facing structural biologists wo  ...[more]

Similar Datasets

| S-EPMC4921272 | biostudies-literature
| S-EPMC4905557 | biostudies-literature
| S-EPMC2917260 | biostudies-literature
| S-EPMC3588912 | biostudies-literature
| S-EPMC5035060 | biostudies-literature
| S-EPMC29619 | biostudies-literature
| S-EPMC10054308 | biostudies-literature
| S-EPMC4366374 | biostudies-literature
| S-EPMC3920302 | biostudies-literature
| S-EPMC4396153 | biostudies-other