Cargando…

ProFace: a server for the analysis of the physicochemical features of protein-protein interfaces

BACKGROUND: Molecular recognition is all pervasive in biology. Protein molecules are involved in enzyme regulation, immune response, signal transduction, oligomer assembly, etc. Delineation of physical and chemical features of the interface formed by protein-protein association would allow us to bet...

Descripción completa

Detalles Bibliográficos
Autores principales: Saha, Rudra P, Bahadur, Ranjit P, Pal, Arumay, Mandal, Saptarshi, Chakrabarti, Pinak
Formato: Texto
Lenguaje:English
Publicado: BioMed Central 2006
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1513576/
https://www.ncbi.nlm.nih.gov/pubmed/16759379
http://dx.doi.org/10.1186/1472-6807-6-11
_version_ 1782128506837139456
author Saha, Rudra P
Bahadur, Ranjit P
Pal, Arumay
Mandal, Saptarshi
Chakrabarti, Pinak
author_facet Saha, Rudra P
Bahadur, Ranjit P
Pal, Arumay
Mandal, Saptarshi
Chakrabarti, Pinak
author_sort Saha, Rudra P
collection PubMed
description BACKGROUND: Molecular recognition is all pervasive in biology. Protein molecules are involved in enzyme regulation, immune response, signal transduction, oligomer assembly, etc. Delineation of physical and chemical features of the interface formed by protein-protein association would allow us to better understand protein interaction networks on one hand, and to design molecules that can engage a given interface and thereby control protein function on the other hand. RESULTS: ProFace is a suite of programs that uses a file, containing atomic coordinates of a multi-chain molecule, as input and analyzes the interface between any two or more subunits. The interface residues are shown segregated into spatial patches (if such a clustering is possible based on an input threshold distance) and/or core and rim regions. A number of physicochemical parameters defining the interface is tabulated. Among the different output files, one contains the list of interacting residues across the interface. Results can be used to infer if a particular interface belongs to a homodimeric molecule. CONCLUSION: A web-server, ProFace (available at ) has been developed for dissecting protein-protein interfaces and deriving various physicochemical parameters.
format Text
id pubmed-1513576
institution National Center for Biotechnology Information
language English
publishDate 2006
publisher BioMed Central
record_format MEDLINE/PubMed
spelling pubmed-15135762006-07-22 ProFace: a server for the analysis of the physicochemical features of protein-protein interfaces Saha, Rudra P Bahadur, Ranjit P Pal, Arumay Mandal, Saptarshi Chakrabarti, Pinak BMC Struct Biol Software BACKGROUND: Molecular recognition is all pervasive in biology. Protein molecules are involved in enzyme regulation, immune response, signal transduction, oligomer assembly, etc. Delineation of physical and chemical features of the interface formed by protein-protein association would allow us to better understand protein interaction networks on one hand, and to design molecules that can engage a given interface and thereby control protein function on the other hand. RESULTS: ProFace is a suite of programs that uses a file, containing atomic coordinates of a multi-chain molecule, as input and analyzes the interface between any two or more subunits. The interface residues are shown segregated into spatial patches (if such a clustering is possible based on an input threshold distance) and/or core and rim regions. A number of physicochemical parameters defining the interface is tabulated. Among the different output files, one contains the list of interacting residues across the interface. Results can be used to infer if a particular interface belongs to a homodimeric molecule. CONCLUSION: A web-server, ProFace (available at ) has been developed for dissecting protein-protein interfaces and deriving various physicochemical parameters. BioMed Central 2006-06-07 /pmc/articles/PMC1513576/ /pubmed/16759379 http://dx.doi.org/10.1186/1472-6807-6-11 Text en Copyright © 2006 Saha et al; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( (http://creativecommons.org/licenses/by/2.0) ), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Software
Saha, Rudra P
Bahadur, Ranjit P
Pal, Arumay
Mandal, Saptarshi
Chakrabarti, Pinak
ProFace: a server for the analysis of the physicochemical features of protein-protein interfaces
title ProFace: a server for the analysis of the physicochemical features of protein-protein interfaces
title_full ProFace: a server for the analysis of the physicochemical features of protein-protein interfaces
title_fullStr ProFace: a server for the analysis of the physicochemical features of protein-protein interfaces
title_full_unstemmed ProFace: a server for the analysis of the physicochemical features of protein-protein interfaces
title_short ProFace: a server for the analysis of the physicochemical features of protein-protein interfaces
title_sort proface: a server for the analysis of the physicochemical features of protein-protein interfaces
topic Software
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1513576/
https://www.ncbi.nlm.nih.gov/pubmed/16759379
http://dx.doi.org/10.1186/1472-6807-6-11
work_keys_str_mv AT saharudrap profaceaserverfortheanalysisofthephysicochemicalfeaturesofproteinproteininterfaces
AT bahadurranjitp profaceaserverfortheanalysisofthephysicochemicalfeaturesofproteinproteininterfaces
AT palarumay profaceaserverfortheanalysisofthephysicochemicalfeaturesofproteinproteininterfaces
AT mandalsaptarshi profaceaserverfortheanalysisofthephysicochemicalfeaturesofproteinproteininterfaces
AT chakrabartipinak profaceaserverfortheanalysisofthephysicochemicalfeaturesofproteinproteininterfaces