RNA-binding protein database

[1] It includes four metazoan species, which are Homo sapiens, Mus musculus, Drosophila melanogaster, and Caenorhabditis elegans.

Because of this, eukaryotes apply a strategy called post-transcriptional modification which includes splicing, editing and polyadenylation to process the pre-mRNA.

As the result, RBPs can bind RNA with higher specificity and affinity than single domain.

In Lunde's article, their group has introduced different types of RNA-binding protein motif and their specific functions.

[7] RNA recognition rotif (RRM) contains about 80–90 amino acids that form four-stranded anti-parallel β-sheet with two helices (βαββαβ topology).

When CCHH zinc finger binds to DNA, residues in its recognition α-helix forming hydrogen bonds to Watson–Crick base pairs in the major groove.

The strategy used by zinc figure to distinguish these two type of nucleotides may contain distinct structural arrangement of this domain.

In their research, one single RBP is incubated with a vast molar excess of a complex pool of RNAs.

The protein is recovered by affinity selection and associated RNAs are interrogated by microarray and computational analyses.

Both ways will lead to the detail information list of proteins which includes gene symbol, annotation ID, synonyms, gene description, species, RNA-binding domain, number of experiment and homologs.

Also, in this database users can search experiments related to specific RNA binding sequence.

Diagram showing crystal structures of RNA-binding proteins; 4 on the top and 2 on the bottom of the image.
Crystallographic structures of RNA-binding domains from RNA-binding proteins.