Cargando…

DISPOT: a simple knowledge-based protein domain interaction statistical potential

MOTIVATION: The complexity of protein–protein interactions (PPIs) is further compounded by the fact that an average protein consists of two or more domains, structurally and evolutionary independent subunits. Experimental studies have demonstrated that an interaction between a pair of proteins is no...

Descripción completa

Detalles Bibliográficos
Autores principales: Narykov, Oleksandr, Bogatov, Dmytro, Korkin, Dmitry
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Oxford University Press 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6954640/
https://www.ncbi.nlm.nih.gov/pubmed/31350874
http://dx.doi.org/10.1093/bioinformatics/btz587
_version_ 1783486837832024064
author Narykov, Oleksandr
Bogatov, Dmytro
Korkin, Dmitry
author_facet Narykov, Oleksandr
Bogatov, Dmytro
Korkin, Dmitry
author_sort Narykov, Oleksandr
collection PubMed
description MOTIVATION: The complexity of protein–protein interactions (PPIs) is further compounded by the fact that an average protein consists of two or more domains, structurally and evolutionary independent subunits. Experimental studies have demonstrated that an interaction between a pair of proteins is not carried out by all domains constituting each protein, but rather by a select subset. However, determining which domains from each protein mediate the corresponding PPI is a challenging task. RESULTS: Here, we present domain interaction statistical potential (DISPOT), a simple knowledge-based statistical potential that estimates the propensity of an interaction between a pair of protein domains, given their structural classification of protein (SCOP) family annotations. The statistical potential is derived based on the analysis of >352 000 structurally resolved PPIs obtained from DOMMINO, a comprehensive database of structurally resolved macromolecular interactions. AVAILABILITY AND IMPLEMENTATION: DISPOT is implemented in Python 2.7 and packaged as an open-source tool. DISPOT is implemented in two modes, basic and auto-extraction. The source code for both modes is available on GitHub: https://github.com/korkinlab/dispot and standalone docker images on DockerHub: https://hub.docker.com/r/korkinlab/dispot. The web server is freely available at http://dispot.korkinlab.org/. SUPPLEMENTARY INFORMATION: Supplementary data are available at Bioinformatics online.
format Online
Article
Text
id pubmed-6954640
institution National Center for Biotechnology Information
language English
publishDate 2019
publisher Oxford University Press
record_format MEDLINE/PubMed
spelling pubmed-69546402020-01-16 DISPOT: a simple knowledge-based protein domain interaction statistical potential Narykov, Oleksandr Bogatov, Dmytro Korkin, Dmitry Bioinformatics Applications Notes MOTIVATION: The complexity of protein–protein interactions (PPIs) is further compounded by the fact that an average protein consists of two or more domains, structurally and evolutionary independent subunits. Experimental studies have demonstrated that an interaction between a pair of proteins is not carried out by all domains constituting each protein, but rather by a select subset. However, determining which domains from each protein mediate the corresponding PPI is a challenging task. RESULTS: Here, we present domain interaction statistical potential (DISPOT), a simple knowledge-based statistical potential that estimates the propensity of an interaction between a pair of protein domains, given their structural classification of protein (SCOP) family annotations. The statistical potential is derived based on the analysis of >352 000 structurally resolved PPIs obtained from DOMMINO, a comprehensive database of structurally resolved macromolecular interactions. AVAILABILITY AND IMPLEMENTATION: DISPOT is implemented in Python 2.7 and packaged as an open-source tool. DISPOT is implemented in two modes, basic and auto-extraction. The source code for both modes is available on GitHub: https://github.com/korkinlab/dispot and standalone docker images on DockerHub: https://hub.docker.com/r/korkinlab/dispot. The web server is freely available at http://dispot.korkinlab.org/. SUPPLEMENTARY INFORMATION: Supplementary data are available at Bioinformatics online. Oxford University Press 2019-12-15 2019-07-27 /pmc/articles/PMC6954640/ /pubmed/31350874 http://dx.doi.org/10.1093/bioinformatics/btz587 Text en © The Author(s) 2019. Published by Oxford University Press. http://creativecommons.org/licenses/by-nc/4.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com
spellingShingle Applications Notes
Narykov, Oleksandr
Bogatov, Dmytro
Korkin, Dmitry
DISPOT: a simple knowledge-based protein domain interaction statistical potential
title DISPOT: a simple knowledge-based protein domain interaction statistical potential
title_full DISPOT: a simple knowledge-based protein domain interaction statistical potential
title_fullStr DISPOT: a simple knowledge-based protein domain interaction statistical potential
title_full_unstemmed DISPOT: a simple knowledge-based protein domain interaction statistical potential
title_short DISPOT: a simple knowledge-based protein domain interaction statistical potential
title_sort dispot: a simple knowledge-based protein domain interaction statistical potential
topic Applications Notes
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6954640/
https://www.ncbi.nlm.nih.gov/pubmed/31350874
http://dx.doi.org/10.1093/bioinformatics/btz587
work_keys_str_mv AT narykovoleksandr dispotasimpleknowledgebasedproteindomaininteractionstatisticalpotential
AT bogatovdmytro dispotasimpleknowledgebasedproteindomaininteractionstatisticalpotential
AT korkindmitry dispotasimpleknowledgebasedproteindomaininteractionstatisticalpotential