Data · dataset · 2015
Molecular architecture of protein-RNA recognition sites
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The molecular architecture of protein-RNA interfaces are analyzed using a non-redundant dataset of 152 protein-RNA complexes.
Description
We find that an average protein-RNA interface is smaller than an average protein-DNA interface but larger than an average protein–protein interface. Among the different classes of protein-RNA complexes, interfaces with tRNA are the largest, while the interfaces with the single-stranded RNA are the smallest.
Significantly, RNA contributes more to the interface area than its partner protein. Moreover, unlike protein–protein interfaces where the side chain contributes less to the interface area compared to the main chain, the main chain and side chain contributions flipped in protein-RNA interfaces. We find that the protein surface in contact with the RNA in protein-RNA complexes is better packed than that in contact with the DNA in protein-DNA complexes, but loosely packed than that in contact with the protein in protein–protein complexes.
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Shape complementarity and electrostatic potential are the two major factors that determine the specificity of the protein-RNA interaction. We find that the H-bond density at the protein-RNA interfaces is similar with that of protein-DNA interfaces but higher than the protein–protein interfaces. Unlike protein-DNA interfaces where the deoxyribose has little role in intermolecular H-bonds, due to the presence of an oxygen atom at the 2′ position, the ribose in RNA plays significant role in protein-RNA H-bonds.
We find that besides H-bonds, salt bridges and stacking interactions also play significant role in stabilizing protein-nucleic acids interfaces; however, their contribution at the protein–protein interfaces is insignificant.
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- Repository landing page tandf.figshare.com/articles/dataset/Molecular_architecture_of_protein_RNA_recogni… ↗
landing page · from DataCite
- Repository landing page tandf.figshare.com/articles/dataset/Molecular_architecture_of_protein_RNA_recogni… ↗
landing page · from DataCite
- DOI doi.org/10.6084/m9.figshare.1305735 ↗
DOI / persistent id · from DataCite
- DOI doi.org/10.6084/m9.figshare.1305735.v1 ↗
DOI / persistent id · from DataCite
Documentation and papers
- Creative Commons Attribution 4.0 International creativecommons.org/licenses/by/4.0/legalcode ↗
license · from DataCite
- IsSupplementTo 10.1080/07391102.2015.1004652 doi.org/10.1080/07391102.2015.1004652 ↗
publication · from DataCite
Catalogue records · 4
- DataCite API api.datacite.org/dois/10.6084/m9.figshare.1305735.v1 ↗
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- DataCite API api.datacite.org/dois/10.6084/m9.figshare.1305735 ↗
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- DataCite Commons commons.datacite.org/doi.org/10.6084/m9.figshare.1305735.v1 ↗
catalogue entry · from DataCite
- DataCite Commons commons.datacite.org/doi.org/10.6084/m9.figshare.1305735 ↗
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Topics
- Stated by source
- Biological sciences · Biological sciences · Chemical sciences · Chemical sciences · Health sciences · Health sciences
- From keywords
- Biochemistry and cell biology · Cancer · Cancer · Genetics · Inorganic chemistry · Physics · Physics
Provenance · 2 source records, 18 field assertions
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|---|---|---|---|
| DataCite | 10.6084/m9.figshare.1305735 | 14 d ago | JSON v1 |
| DataCite | 10.6084/m9.figshare.1305735.v1 | 14 d ago | JSON v1 |
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