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LenVarDB: database of length-variant protein domains

Protein domains are functionally and structurally independent modules, which add to the functional variety of proteins. This array of functional diversity has been enabled by evolutionary changes, such as amino acid substitutions or insertions or deletions, occurring in these protein domains. Length...

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Autores principales: Mutt, Eshita, Mathew, Oommen K., Sowdhamini, Ramanathan
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Oxford University Press 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3964994/
https://www.ncbi.nlm.nih.gov/pubmed/24194591
http://dx.doi.org/10.1093/nar/gkt1014
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author Mutt, Eshita
Mathew, Oommen K.
Sowdhamini, Ramanathan
author_facet Mutt, Eshita
Mathew, Oommen K.
Sowdhamini, Ramanathan
author_sort Mutt, Eshita
collection PubMed
description Protein domains are functionally and structurally independent modules, which add to the functional variety of proteins. This array of functional diversity has been enabled by evolutionary changes, such as amino acid substitutions or insertions or deletions, occurring in these protein domains. Length variations (indels) can introduce changes at structural, functional and interaction levels. LenVarDB (freely available at http://caps.ncbs.res.in/lenvardb/) traces these length variations, starting from structure-based sequence alignments in our Protein Alignments organized as Structural Superfamilies (PASS2) database, across 731 structural classification of proteins (SCOP)-based protein domain superfamilies connected to 2 730 625 sequence homologues. Alignment of sequence homologues corresponding to a structural domain is available, starting from a structure-based sequence alignment of the superfamily. Orientation of the length-variant (indel) regions in protein domains can be visualized by mapping them on the structure and on the alignment. Knowledge about location of length variations within protein domains and their visual representation will be useful in predicting changes within structurally or functionally relevant sites, which may ultimately regulate protein function. Non-technical summary: Evolutionary changes bring about natural changes to proteins that may be found in many organisms. Such changes could be reflected as amino acid substitutions or insertions–deletions (indels) in protein sequences. LenVarDB is a database that provides an early overview of observed length variations that were set among 731 protein families and after examining >2 million sequences. Indels are followed up to observe if they are close to the active site such that they can affect the activity of proteins. Inclusion of such information can aid the design of bioengineering experiments.
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spelling pubmed-39649942014-03-25 LenVarDB: database of length-variant protein domains Mutt, Eshita Mathew, Oommen K. Sowdhamini, Ramanathan Nucleic Acids Res II. Protein sequence and structure, motifs and domains Protein domains are functionally and structurally independent modules, which add to the functional variety of proteins. This array of functional diversity has been enabled by evolutionary changes, such as amino acid substitutions or insertions or deletions, occurring in these protein domains. Length variations (indels) can introduce changes at structural, functional and interaction levels. LenVarDB (freely available at http://caps.ncbs.res.in/lenvardb/) traces these length variations, starting from structure-based sequence alignments in our Protein Alignments organized as Structural Superfamilies (PASS2) database, across 731 structural classification of proteins (SCOP)-based protein domain superfamilies connected to 2 730 625 sequence homologues. Alignment of sequence homologues corresponding to a structural domain is available, starting from a structure-based sequence alignment of the superfamily. Orientation of the length-variant (indel) regions in protein domains can be visualized by mapping them on the structure and on the alignment. Knowledge about location of length variations within protein domains and their visual representation will be useful in predicting changes within structurally or functionally relevant sites, which may ultimately regulate protein function. Non-technical summary: Evolutionary changes bring about natural changes to proteins that may be found in many organisms. Such changes could be reflected as amino acid substitutions or insertions–deletions (indels) in protein sequences. LenVarDB is a database that provides an early overview of observed length variations that were set among 731 protein families and after examining >2 million sequences. Indels are followed up to observe if they are close to the active site such that they can affect the activity of proteins. Inclusion of such information can aid the design of bioengineering experiments. Oxford University Press 2014-01-01 2013-11-03 /pmc/articles/PMC3964994/ /pubmed/24194591 http://dx.doi.org/10.1093/nar/gkt1014 Text en © The Author(s) 2013. Published by Oxford University Press. http://creativecommons.org/licenses/by/3.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by/3.0/), which permits non-commercial reuse, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com
spellingShingle II. Protein sequence and structure, motifs and domains
Mutt, Eshita
Mathew, Oommen K.
Sowdhamini, Ramanathan
LenVarDB: database of length-variant protein domains
title LenVarDB: database of length-variant protein domains
title_full LenVarDB: database of length-variant protein domains
title_fullStr LenVarDB: database of length-variant protein domains
title_full_unstemmed LenVarDB: database of length-variant protein domains
title_short LenVarDB: database of length-variant protein domains
title_sort lenvardb: database of length-variant protein domains
topic II. Protein sequence and structure, motifs and domains
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3964994/
https://www.ncbi.nlm.nih.gov/pubmed/24194591
http://dx.doi.org/10.1093/nar/gkt1014
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