MutaBind estimates and interprets the effects of sequence variants on protein-protein interactions
- Autores
- Li, Minghui; Simonetti, Franco Lucio; Goncearenco, Alexander; Panchenko, Anna R.
- Año de publicación
- 2016
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- Proteins engage in highly selective interactions with their macromolecular partners. Sequence variants that alter protein binding affinity may cause significant perturbations or complete abolishment of function, potentially leading to diseases. There exists a persistent need to develop a mechanistic understanding of impacts of variants on proteins. To address this need we introduce a new computational method MutaBind to evaluate the effects of sequence variants and disease mutations on protein interactions and calculate the quantitative changes in binding affinity. The MutaBind method uses molecular mechanics force fields, statistical potentials and fast side-chain optimization algorithms. The MutaBind server maps mutations on a structural protein complex, calculates the associated changes in binding affinity, determines the deleterious effect of a mutation, estimates the confidence of this prediction and produces a mutant structural model for download. MutaBind can be applied to a large number of problems, including determination of potential driver mutations in cancer and other diseases, elucidation of the effects of sequence variants on protein fitness in evolution and protein design. MutaBind is available at http://www.ncbi.nlm.nih.gov/projects/mutabind/.
Fil: Li, Minghui. National Institutes Of Health; Estados Unidos
Fil: Simonetti, Franco Lucio. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina
Fil: Goncearenco, Alexander. National Institutes Of Health; Estados Unidos
Fil: Panchenko, Anna R.. National Institutes Of Health; Estados Unidos - Materia
-
PROTEIN PROTEIN INTERACTION
MUTATION
SEQUENCE VARIANTS
SERVER - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
- Repositorio
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/18159
Ver los metadatos del registro completo
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MutaBind estimates and interprets the effects of sequence variants on protein-protein interactionsLi, MinghuiSimonetti, Franco LucioGoncearenco, AlexanderPanchenko, Anna R.PROTEIN PROTEIN INTERACTIONMUTATIONSEQUENCE VARIANTSSERVERhttps://purl.org/becyt/ford/1.2https://purl.org/becyt/ford/1Proteins engage in highly selective interactions with their macromolecular partners. Sequence variants that alter protein binding affinity may cause significant perturbations or complete abolishment of function, potentially leading to diseases. There exists a persistent need to develop a mechanistic understanding of impacts of variants on proteins. To address this need we introduce a new computational method MutaBind to evaluate the effects of sequence variants and disease mutations on protein interactions and calculate the quantitative changes in binding affinity. The MutaBind method uses molecular mechanics force fields, statistical potentials and fast side-chain optimization algorithms. The MutaBind server maps mutations on a structural protein complex, calculates the associated changes in binding affinity, determines the deleterious effect of a mutation, estimates the confidence of this prediction and produces a mutant structural model for download. MutaBind can be applied to a large number of problems, including determination of potential driver mutations in cancer and other diseases, elucidation of the effects of sequence variants on protein fitness in evolution and protein design. MutaBind is available at http://www.ncbi.nlm.nih.gov/projects/mutabind/.Fil: Li, Minghui. National Institutes Of Health; Estados UnidosFil: Simonetti, Franco Lucio. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; ArgentinaFil: Goncearenco, Alexander. National Institutes Of Health; Estados UnidosFil: Panchenko, Anna R.. National Institutes Of Health; Estados UnidosOxford University Press2016-05info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/18159Li, Minghui; Simonetti, Franco Lucio; Goncearenco, Alexander; Panchenko, Anna R.; MutaBind estimates and interprets the effects of sequence variants on protein-protein interactions; Oxford University Press; Nucleic Acids Research; 44; W1; 5-2016; W494-5010305-10481362-4962CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://academic.oup.com/nar/article-lookup/doi/10.1093/nar/gkw374info:eu-repo/semantics/altIdentifier/doi/10.1093/nar/gkw374info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:18:25Zoai:ri.conicet.gov.ar:11336/18159instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-29 10:18:25.769CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
MutaBind estimates and interprets the effects of sequence variants on protein-protein interactions |
title |
MutaBind estimates and interprets the effects of sequence variants on protein-protein interactions |
spellingShingle |
MutaBind estimates and interprets the effects of sequence variants on protein-protein interactions Li, Minghui PROTEIN PROTEIN INTERACTION MUTATION SEQUENCE VARIANTS SERVER |
title_short |
MutaBind estimates and interprets the effects of sequence variants on protein-protein interactions |
title_full |
MutaBind estimates and interprets the effects of sequence variants on protein-protein interactions |
title_fullStr |
MutaBind estimates and interprets the effects of sequence variants on protein-protein interactions |
title_full_unstemmed |
MutaBind estimates and interprets the effects of sequence variants on protein-protein interactions |
title_sort |
MutaBind estimates and interprets the effects of sequence variants on protein-protein interactions |
dc.creator.none.fl_str_mv |
Li, Minghui Simonetti, Franco Lucio Goncearenco, Alexander Panchenko, Anna R. |
author |
Li, Minghui |
author_facet |
Li, Minghui Simonetti, Franco Lucio Goncearenco, Alexander Panchenko, Anna R. |
author_role |
author |
author2 |
Simonetti, Franco Lucio Goncearenco, Alexander Panchenko, Anna R. |
author2_role |
author author author |
dc.subject.none.fl_str_mv |
PROTEIN PROTEIN INTERACTION MUTATION SEQUENCE VARIANTS SERVER |
topic |
PROTEIN PROTEIN INTERACTION MUTATION SEQUENCE VARIANTS SERVER |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/1.2 https://purl.org/becyt/ford/1 |
dc.description.none.fl_txt_mv |
Proteins engage in highly selective interactions with their macromolecular partners. Sequence variants that alter protein binding affinity may cause significant perturbations or complete abolishment of function, potentially leading to diseases. There exists a persistent need to develop a mechanistic understanding of impacts of variants on proteins. To address this need we introduce a new computational method MutaBind to evaluate the effects of sequence variants and disease mutations on protein interactions and calculate the quantitative changes in binding affinity. The MutaBind method uses molecular mechanics force fields, statistical potentials and fast side-chain optimization algorithms. The MutaBind server maps mutations on a structural protein complex, calculates the associated changes in binding affinity, determines the deleterious effect of a mutation, estimates the confidence of this prediction and produces a mutant structural model for download. MutaBind can be applied to a large number of problems, including determination of potential driver mutations in cancer and other diseases, elucidation of the effects of sequence variants on protein fitness in evolution and protein design. MutaBind is available at http://www.ncbi.nlm.nih.gov/projects/mutabind/. Fil: Li, Minghui. National Institutes Of Health; Estados Unidos Fil: Simonetti, Franco Lucio. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina Fil: Goncearenco, Alexander. National Institutes Of Health; Estados Unidos Fil: Panchenko, Anna R.. National Institutes Of Health; Estados Unidos |
description |
Proteins engage in highly selective interactions with their macromolecular partners. Sequence variants that alter protein binding affinity may cause significant perturbations or complete abolishment of function, potentially leading to diseases. There exists a persistent need to develop a mechanistic understanding of impacts of variants on proteins. To address this need we introduce a new computational method MutaBind to evaluate the effects of sequence variants and disease mutations on protein interactions and calculate the quantitative changes in binding affinity. The MutaBind method uses molecular mechanics force fields, statistical potentials and fast side-chain optimization algorithms. The MutaBind server maps mutations on a structural protein complex, calculates the associated changes in binding affinity, determines the deleterious effect of a mutation, estimates the confidence of this prediction and produces a mutant structural model for download. MutaBind can be applied to a large number of problems, including determination of potential driver mutations in cancer and other diseases, elucidation of the effects of sequence variants on protein fitness in evolution and protein design. MutaBind is available at http://www.ncbi.nlm.nih.gov/projects/mutabind/. |
publishDate |
2016 |
dc.date.none.fl_str_mv |
2016-05 |
dc.type.none.fl_str_mv |
info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion http://purl.org/coar/resource_type/c_6501 info:ar-repo/semantics/articulo |
format |
article |
status_str |
publishedVersion |
dc.identifier.none.fl_str_mv |
http://hdl.handle.net/11336/18159 Li, Minghui; Simonetti, Franco Lucio; Goncearenco, Alexander; Panchenko, Anna R.; MutaBind estimates and interprets the effects of sequence variants on protein-protein interactions; Oxford University Press; Nucleic Acids Research; 44; W1; 5-2016; W494-501 0305-1048 1362-4962 CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/18159 |
identifier_str_mv |
Li, Minghui; Simonetti, Franco Lucio; Goncearenco, Alexander; Panchenko, Anna R.; MutaBind estimates and interprets the effects of sequence variants on protein-protein interactions; Oxford University Press; Nucleic Acids Research; 44; W1; 5-2016; W494-501 0305-1048 1362-4962 CONICET Digital CONICET |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/url/https://academic.oup.com/nar/article-lookup/doi/10.1093/nar/gkw374 info:eu-repo/semantics/altIdentifier/doi/10.1093/nar/gkw374 |
dc.rights.none.fl_str_mv |
info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ |
eu_rights_str_mv |
openAccess |
rights_invalid_str_mv |
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ |
dc.format.none.fl_str_mv |
application/pdf application/pdf application/pdf |
dc.publisher.none.fl_str_mv |
Oxford University Press |
publisher.none.fl_str_mv |
Oxford University Press |
dc.source.none.fl_str_mv |
reponame:CONICET Digital (CONICET) instname:Consejo Nacional de Investigaciones Científicas y Técnicas |
reponame_str |
CONICET Digital (CONICET) |
collection |
CONICET Digital (CONICET) |
instname_str |
Consejo Nacional de Investigaciones Científicas y Técnicas |
repository.name.fl_str_mv |
CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas |
repository.mail.fl_str_mv |
dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar |
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1844614146008547328 |
score |
13.070432 |