ArticleNucleic acids research2010
CCRXP: exploring clusters of conserved residues in protein structures.
Article in Nucleic acids research, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 14 citations in OpenAlex.
- Host-pathogen protein-nucleic acid interactions: A comprehensive review.Computational and structural biotechnology journal · 2022Review
- Analyses on clustering of the conserved residues at protein-RNA interfaces and its application in binding site identification.BMC bioinformatics · 2020Article
- Interolog interfaces in protein-protein docking.Proteins · 2015Article
- Discrete structural features among interface residue-level classes.BMC bioinformatics · 2015Article
- Communication routes in ARID domains between distal residues in helix 5 and the DNA-binding loops.PLoS computational biology · 2014Article
- SPRITE and ASSAM: web servers for side chain 3D-motif searching in protein structures.Nucleic acids research · 2012Article
- HotRegion: a database of predicted hot spot clusters.Nucleic acids research · 2012Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Conserved residues forming tightly packed clusters have been shown to be energy hot spots in both protein-protein and protein-DNA complexes. A number of analyses on these clusters of conserved residues (CCRs) have been reported, all pointing to a crucial role that these clusters play in protein function, especially protein-protein and protein-DNA interactions. However, currently there is no publicly available tool to automatically detect such clusters. Here, we present a web server that takes a coordinate file in PDB format as input and automatically executes all the steps to identify CCRs in protein structures. In addition, it calculates the structural properties of each residue and of the CCRs. We also present statistics to show that CCRs, determined by these procedures, are significantly enriched in 'hot spots' in protein-protein and protein-RNA complexes, which supplements our more detailed similar results on protein-DNA complexes. We expect that CCRXP web server will be useful in studies of protein structures and their interactions and selecting mutagenesis targets. The web server can be accessed at http://ccrxp.netasa.org.
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Registered trials
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