Dataset Information

BIPSPI: a method for the prediction of partner-specific protein-protein interfaces.

ABSTRACT: Motivation:Protein-Protein Interactions (PPI) are essentials for most cellular processes and thus, unveiling how proteins interact is a crucial question that can be better understood by identifying which residues are responsible for the interaction. Computational approaches are orders of magnitude cheaper and faster than experimental ones, leading to proliferation of multiple methods aimed to predict which residues belong to the interface of an interaction. Results:We present BIPSPI, a new machine learning-based method for the prediction of partner-specific PPI sites. Contrary to most binding site prediction methods, the proposed approach takes into account a pair of interacting proteins rather than a single one in order to predict partner-specific binding sites. BIPSPI has been trained employing sequence-based and structural features from both protein partners of each complex compiled in the Protein-Protein Docking Benchmark version 5.0 and in an additional set independently compiled. Also, a version trained only on sequences has been developed. The performance of our approach has been assessed by a leave-one-out cross-validation over different benchmarks, outperforming state-of-the-art methods. Availability and implementation:BIPSPI web server is freely available at http://bipspi.cnb.csic.es. BIPSPI code is available at https://github.com/bioinsilico/BIPSPI. Docker image is available at https://hub.docker.com/r/bioinsilico/bipspi/. Supplementary information:Supplementary data are available at Bioinformatics online.

SUBMITTER: Sanchez-Garcia R

PROVIDER: S-EPMC6361243 | biostudies-literature | 2019 Feb

REPOSITORIES: biostudies-literature

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BIPSPI: a method for the prediction of partner-specific protein-protein interfaces.

Sanchez-Garcia Ruben R Sorzano C O S COS Carazo J M JM Segura Joan J

Bioinformatics (Oxford, England) 20190201 3

<h4>Motivation</h4>Protein-Protein Interactions (PPI) are essentials for most cellular processes and thus, unveiling how proteins interact is a crucial question that can be better understood by identifying which residues are responsible for the interaction. Computational approaches are orders of magnitude cheaper and faster than experimental ones, leading to proliferation of multiple methods aimed to predict which residues belong to the interface of an interaction.<h4>Results</h4>We present BIPS ...[more]

PMID: 30020406

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Project description:MotivationAccurate predictions of protein-binding residues (PBRs) enhances understanding of molecular-level rules governing protein-protein interactions, helps protein-protein docking and facilitates annotation of protein functions. Recent studies show that current sequence-based predictors of PBRs severely cross-predict residues that interact with other types of protein partners (e.g. RNA and DNA) as PBRs. Moreover, these methods are relatively slow, prohibiting genome-scale use.ResultsWe propose a novel, accurate and fast sequence-based predictor of PBRs that minimizes the cross-predictions. Our SCRIBER (SeleCtive pRoteIn-Binding rEsidue pRedictor) method takes advantage of three innovations: comprehensive dataset that covers multiple types of binding residues, novel types of inputs that are relevant to the prediction of PBRs, and an architecture that is tailored to reduce the cross-predictions. The dataset includes complete protein chains and offers improved coverage of binding annotations that are transferred from multiple protein-protein complexes. We utilize innovative two-layer architecture where the first layer generates a prediction of protein-binding, RNA-binding, DNA-binding and small ligand-binding residues. The second layer re-predicts PBRs by reducing overlap between PBRs and the other types of binding residues produced in the first layer. Empirical tests on an independent test dataset reveal that SCRIBER significantly outperforms current predictors and that all three innovations contribute to its high predictive performance. SCRIBER reduces cross-predictions by between 41% and 69% and our conservative estimates show that it is at least 3 times faster. We provide putative PBRs produced by SCRIBER for the entire human proteome and use these results to hypothesize that about 14% of currently known human protein domains bind proteins.Availability and implementationSCRIBER webserver is available at http://biomine.cs.vcu.edu/servers/SCRIBER/.Supplementary informationSupplementary data are available at Bioinformatics online.

Dataset Information

BIPSPI: a method for the prediction of partner-specific protein-protein interfaces.

Publications

BIPSPI: a method for the prediction of partner-specific protein-protein interfaces.

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