Document Type
Article
Publication Date
2010
Keywords
Reverse, Retro, Invert, Alignment, Intrinsic Disorder, PONDR-RIBS
Digital Object Identifier (DOI)
https://doi.org/10.3390/ijms11103725
Abstract
Many cell functions in all living organisms rely on protein-based molecular recognition involving disorder-to-order transitions upon binding by molecular recognition features (MoRFs). A well accepted computational tool for identifying likely protein-protein interactions is sequence alignment. In this paper, we propose the combination of sequence alignment and disorder prediction as a tool to improve the confidence of identifying MoRF-based protein-protein interactions. The method of reverse sequence alignment is also rationalized here as a novel approach for finding additional interaction regions, leading to the concept of a retro-MoRF, which has the reversed sequence of an identified MoRF. The set of retro-MoRF binding partners likely overlap the partner-sets of the originally identified MoRFs. The high abundance of MoRF-containing intrinsically disordered proteins in nature suggests the possibility that the number of retro-MoRFs could likewise be very high. This hypothesis provides new grounds for exploring the mysteries of protein-protein interaction networks at the genome level.
Rights Information
This work is licensed under a Creative Commons Attribution 3.0 License.
Was this content written or created while at USF?
Yes
Citation / Publisher Attribution
International Journal of Molecular Sciences, v. 11, issue 10, p. 3725-3747
Scholar Commons Citation
Xue, Bin; Dunker, A. Keith; and Uversky, Vladimir N., "Retro-MoRFs: Identifying Protein Binding Sites by Normal and Reverse Alignment and Intrinsic Disorder Prediction" (2010). Molecular Medicine Faculty Publications. 471.
https://digitalcommons.usf.edu/mme_facpub/471
