![[feed]](/style/images/feed-icon-14x14.png){kind=icon}
Tools
Tools
![[thumbnail of 13702oa.pdf]](https://edoc.mdc-berlin.de/style/images/fileicons/application_pdf.png) |
PDF
- Requires a PDF viewer such as GSview, Xpdf or Adobe Acrobat Reader
1MB |
| Item Type: | Article |
|---|---|
| Title: | Functional and genomic analyses of α-solenoid proteins |
| Creators Name: | Fournier, D., Palidwor, G.A., Shcherbinin, S., Szengel, A., Schaefer, M.H., Perez-Iratxeta, C. and Andrade-Navarro, M.A. |
| Abstract: | {alpha}-solenoids are flexible protein structural domains formed by ensembles of alpha-helical repeats (Armadillo and HEAT repeats among others). While homology can be used to detect many of these repeats, some {alpha}-solenoids have very little sequence homology to proteins of known structure and we expect that many remain undetected. We previously developed a method for detection of {alpha}-helical repeats based on a neural network trained on a dataset of protein structures. Here we improved the detection algorithm and updated the training dataset using recently solved structures of {alpha}-solenoids. Unexpectedly, we identified occurrences of {alpha}-solenoids in solved protein structures that escaped attention, for example within the core of the catalytic subunit of PI3KC. Our results expand the current set of known {alpha}-solenoids. Application of our tool to the protein universe allowed us to detect their significant enrichment in proteins interacting with many proteins, confirming that {alpha}-solenoids are generally involved in protein-protein interactions. We then studied the taxonomic distribution of {alpha}-solenoids to discuss an evolutionary scenario for the emergence of this type of domain, speculating that {alpha}-solenoids have emerged in multiple taxa in independent events by convergent evolution. We observe a higher rate of {alpha}-solenoids in eukaryotic genomes and in some prokaryotic families, such as Cyanobacteria and Planctomycetes, which could be associated to increased cellular complexity. The method is available at http://cbdm.mdc-berlin.de/~ard2/. |
| Keywords: | Genomics, Protein Conformation, Proteins |
| Source: | PLoS ONE |
| ISSN: | 1932-6203 |
| Publisher: | Public Library of Science |
| Volume: | 8 |
| Number: | 11 |
| Page Range: | e79894 |
| Date: | 21 November 2013 |
| Official Publication: | https://doi.org/10.1371/journal.pone.0079894 |
| PubMed: | View item in PubMed |
Repository Staff Only: item control page
