ArticleJournal of structural and functional genomics2011
PRICE (PRotein Interface Conservation and Energetics): a server for the analysis of protein-protein interfaces.
Article in Journal of structural and functional genomics, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- ProDFace: A web-tool for the dissection of protein-DNA interfaces.Frontiers in molecular biosciences · 2022Article
- Article
- A Machine Learning Approach for Hot-Spot Detection at Protein-Protein Interfaces.International journal of molecular sciences · 2016Article
- A structural dissection of large protein-protein crystal packing contacts.Scientific reports · 2015Article
- Contribution of cation-π interactions to the stability of Sm/LSm oligomeric assemblies.Protoplasma · 2015Article
- On the binding affinity of macromolecular interactions: daring to ask why proteins interact.Journal of the Royal Society, Interface · 2013Review
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Authors and funding
4 authors.
Funding
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Abstract
Residues in a protein-protein interface that are important for forming and stabilizing the interaction can usually be identified by looking at patterns of evolutionary conservation in groups of homologous proteins and also by the computational identification of binding hotspots. The PRICE (PRotein Interface Conservation and Energetics) server takes the coordinates of a protein-protein complex, dissects the interface into core and rim regions, and calculates (1) the degree of conservation (measured as the sequence entropy), as well as (2) the change in free energy of binding (∆∆G, due to alanine scanning mutagenesis) of interface residues. Results are displayed as color-coded plots and also made available for download. This enables the computational identification of binding hot spots, based on which further experiments can be designed. The method will aid in protein functional prediction by correct assignment of hot regions involved in binding. Consideration of sequence entropies for residues with large ∆∆G values may provide an indication of the biological relevance of the interface. Finally, the results obtained on a test set of alanine mutants has been compared to those obtained using other servers/methods. The PRICE server is a web application available at http://www.boseinst.ernet.in/resources/bioinfo/stag.html.
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Registered trials
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