CORDAX web server: an online platform for the prediction and 3D visualization of aggregation motifs in protein sequences
Year: 2024
Type: article
Abstract: MOTIVATION: Proteins, the molecular workhorses of biological systems, execute a multitude of critical functions dictated by their precise three-dimensional structures. In a complex and dynamic cellular environment, proteins can undergo misfolding, leading to the formation of aggregates that take up various forms, including amorphous and ordered aggregation in the shape of amyloid fibrils. This phenomenon is closely linked to a spectrum of widespread debilitating pathologies, such as Alzheimer's disease, Parkinson's disease, type-II diabetes, and several other proteinopathies, but also hampers the engineering of soluble agents, as in the case of antibody development. As such, the accurate prediction of aggregation propensity within protein sequences has become pivotal due to profound implications in understanding disease mechanisms, as well as in improving biotechnological and therapeutic applications. RESULTS: We previously developed Cordax, a structure-based predictor that utilizes logistic regression to detect aggregation motifs in protein sequences based on their structural complementarity to the amyloid cross-beta architecture. Here, we present a dedicated web server interface for Cordax. This online platform combines several features including detailed scoring of sequence aggregation propensity, as well as 3D visualization with several customization options for topology models of the structural cores formed by predicted aggregation motifs. In addition, information is provided on experimentally determined aggregation-prone regions that exhibit sequence similarity to predicted motifs, scores, and links to other predictor outputs, as well as simultaneous predictions of relevant sequence propensities, such as solubility, hydrophobicity, and secondary structure propensity. AVAILABILITY AND IMPLEMENTATION: The Cordax webserver is freely accessible at https://cordax.switchlab.org/.
Source: Bioinformatics
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: gold
Estimated APC paid: $4,188
Awards: G2475798000, Heterotypic amyloid interactions as modulators of selective cellular vulnerability, Mapping the impact of post-translational modifications on protein aggregation., G491962258, A high-throughput platform for screening amyloid strains and their seeding capacity at single-particle resolution, Principles of specificity in cross-aggregation interactions, Cellular handling of protein aggregation gatekeepers, G8248501640, Towards understanding the specificity of protein aggregation, G8524111995, Heterotypic amyloid interactions as modulators of selective cellular vulnerability
OpenAlex ID: W4395118065