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BindML/BindML+: Detecting Protein-Protein Interaction Interface Propensity from Amino Acid Substitution Patterns.

Authors :
Wei Q
La D
Kihara D
Source :
Methods in molecular biology (Clifton, N.J.) [Methods Mol Biol] 2017; Vol. 1529, pp. 279-289.
Publication Year :
2017

Abstract

Prediction of protein-protein interaction sites in a protein structure provides important information for elucidating the mechanism of protein function and can also be useful in guiding a modeling or design procedures of protein complex structures. Since prediction methods essentially assess the propensity of amino acids that are likely to be part of a protein docking interface, they can help in designing protein-protein interactions. Here, we introduce BindML and BindML+ protein-protein interaction sites prediction methods. BindML predicts protein-protein interaction sites by identifying mutation patterns found in known protein-protein complexes using phylogenetic substitution models. BindML+ is an extension of BindML for distinguishing permanent and transient types of protein-protein interaction sites. We developed an interactive web-server that provides a convenient interface to assist in structural visualization of protein-protein interactions site predictions. The input data for the web-server are a tertiary structure of interest. BindML and BindML+ are available at http://kiharalab.org/bindml/ and http://kiharalab.org/bindml/plus/ .

Details

Language :
English
ISSN :
1940-6029
Volume :
1529
Database :
MEDLINE
Journal :
Methods in molecular biology (Clifton, N.J.)
Publication Type :
Academic Journal
Accession number :
27914057
Full Text :
https://doi.org/10.1007/978-1-4939-6637-0_14