ChanFAD: A Functional Annotation Database for Ion Channels

Ion channels are integral membrane protein complexes critical for regulation of membrane potential, cell volume, and other signaling events. As complex molecular assemblies with many interacting partners, ion channels have multiple structural and functional domains. While channel sequence and functi...

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Main Authors: Elizabeth V. Castro, John W. Shepherd, Ryan S. Guggenheim, Manimone Sengvoravong, Bailey C. Hall, McKenzie K. Chappell, Jessica A. Hearn, Olivia N. Caraccio, Cora Bissman, Sydney Lantow, Damian Buehner, Harry R. Costlow, David M. Prather, Abigail M. Zonza, Mallory Witt, Jeffrey A. Zahratka
Format: Article
Language:English
Published: Frontiers Media S.A. 2022-07-01
Series:Frontiers in Bioinformatics
Subjects:
Online Access:https://www.frontiersin.org/articles/10.3389/fbinf.2022.835805/full
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author Elizabeth V. Castro
Elizabeth V. Castro
John W. Shepherd
Ryan S. Guggenheim
Ryan S. Guggenheim
Manimone Sengvoravong
Bailey C. Hall
McKenzie K. Chappell
McKenzie K. Chappell
Jessica A. Hearn
Jessica A. Hearn
Olivia N. Caraccio
Cora Bissman
Cora Bissman
Sydney Lantow
Damian Buehner
Harry R. Costlow
David M. Prather
Abigail M. Zonza
Mallory Witt
Jeffrey A. Zahratka
Jeffrey A. Zahratka
author_facet Elizabeth V. Castro
Elizabeth V. Castro
John W. Shepherd
Ryan S. Guggenheim
Ryan S. Guggenheim
Manimone Sengvoravong
Bailey C. Hall
McKenzie K. Chappell
McKenzie K. Chappell
Jessica A. Hearn
Jessica A. Hearn
Olivia N. Caraccio
Cora Bissman
Cora Bissman
Sydney Lantow
Damian Buehner
Harry R. Costlow
David M. Prather
Abigail M. Zonza
Mallory Witt
Jeffrey A. Zahratka
Jeffrey A. Zahratka
author_sort Elizabeth V. Castro
collection DOAJ
description Ion channels are integral membrane protein complexes critical for regulation of membrane potential, cell volume, and other signaling events. As complex molecular assemblies with many interacting partners, ion channels have multiple structural and functional domains. While channel sequence and functional data are readily available across multiple online resources, there is an unmet need for functional annotation directly relating primary sequence information, 2D interactions, and three-dimensional protein structure. To this end, we present ChanFAD (Channel Functional Annotation Database), to provide the research community with a centralized resource for ion channel structure and functional data. ChanFAD provides functional annotation of PDB structures built on the National Center for Biotechnology Information’s iCn3D structure viewing tool while providing additional information such as primary sequence, organism, and relevant links to other databases. Here we provide a brief tour of ChanFAD functionality while showing example use cases involving drug-channel interactions and structural changes based on mutation. ChanFAD is freely available and can be accessed at https://www.chanfad.org/.
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spelling doaj.art-5bc9a44b001049f9b61703c75d62e4f42022-12-22T03:04:39ZengFrontiers Media S.A.Frontiers in Bioinformatics2673-76472022-07-01210.3389/fbinf.2022.835805835805ChanFAD: A Functional Annotation Database for Ion ChannelsElizabeth V. Castro0Elizabeth V. Castro1John W. Shepherd2Ryan S. Guggenheim3Ryan S. Guggenheim4Manimone Sengvoravong5Bailey C. Hall6McKenzie K. Chappell7McKenzie K. Chappell8Jessica A. Hearn9Jessica A. Hearn10Olivia N. Caraccio11Cora Bissman12Cora Bissman13Sydney Lantow14Damian Buehner15Harry R. Costlow16David M. Prather17Abigail M. Zonza18Mallory Witt19Jeffrey A. Zahratka20Jeffrey A. Zahratka21Department of Neuroscience, Baldwin Wallace University, Berea, OH, United StatesDepartment of Psychology, Baldwin Wallace University, Berea, OH, United StatesDepartment of Neuroscience, Baldwin Wallace University, Berea, OH, United StatesDepartment of Neuroscience, Baldwin Wallace University, Berea, OH, United StatesDepartment of Psychology, Baldwin Wallace University, Berea, OH, United StatesDepartment of Neuroscience, Baldwin Wallace University, Berea, OH, United StatesDepartment of Neuroscience, Baldwin Wallace University, Berea, OH, United StatesDepartment of Neuroscience, Baldwin Wallace University, Berea, OH, United StatesDepartment of Biology and Geology, Baldwin Wallace University, Berea, OH, United StatesDepartment of Neuroscience, Baldwin Wallace University, Berea, OH, United StatesDepartment of Biology and Geology, Baldwin Wallace University, Berea, OH, United StatesDepartment of Neuroscience, Baldwin Wallace University, Berea, OH, United StatesDepartment of Neuroscience, Baldwin Wallace University, Berea, OH, United StatesDepartment of Biology and Geology, Baldwin Wallace University, Berea, OH, United StatesDepartment of Neuroscience, Baldwin Wallace University, Berea, OH, United StatesDepartment of Neuroscience, Baldwin Wallace University, Berea, OH, United StatesDepartment of Neuroscience, Baldwin Wallace University, Berea, OH, United StatesDepartment of Chemistry, Baldwin Wallace University, Berea, OH, United StatesDepartment of Biology and Geology, Baldwin Wallace University, Berea, OH, United StatesDepartment of Neuroscience, Baldwin Wallace University, Berea, OH, United StatesDepartment of Neuroscience, Baldwin Wallace University, Berea, OH, United StatesDepartment of Biology and Geology, Baldwin Wallace University, Berea, OH, United StatesIon channels are integral membrane protein complexes critical for regulation of membrane potential, cell volume, and other signaling events. As complex molecular assemblies with many interacting partners, ion channels have multiple structural and functional domains. While channel sequence and functional data are readily available across multiple online resources, there is an unmet need for functional annotation directly relating primary sequence information, 2D interactions, and three-dimensional protein structure. To this end, we present ChanFAD (Channel Functional Annotation Database), to provide the research community with a centralized resource for ion channel structure and functional data. ChanFAD provides functional annotation of PDB structures built on the National Center for Biotechnology Information’s iCn3D structure viewing tool while providing additional information such as primary sequence, organism, and relevant links to other databases. Here we provide a brief tour of ChanFAD functionality while showing example use cases involving drug-channel interactions and structural changes based on mutation. ChanFAD is freely available and can be accessed at https://www.chanfad.org/.https://www.frontiersin.org/articles/10.3389/fbinf.2022.835805/fullion channelsfunctional annotationprotein structuredatabaseproteomics
spellingShingle Elizabeth V. Castro
Elizabeth V. Castro
John W. Shepherd
Ryan S. Guggenheim
Ryan S. Guggenheim
Manimone Sengvoravong
Bailey C. Hall
McKenzie K. Chappell
McKenzie K. Chappell
Jessica A. Hearn
Jessica A. Hearn
Olivia N. Caraccio
Cora Bissman
Cora Bissman
Sydney Lantow
Damian Buehner
Harry R. Costlow
David M. Prather
Abigail M. Zonza
Mallory Witt
Jeffrey A. Zahratka
Jeffrey A. Zahratka
ChanFAD: A Functional Annotation Database for Ion Channels
Frontiers in Bioinformatics
ion channels
functional annotation
protein structure
database
proteomics
title ChanFAD: A Functional Annotation Database for Ion Channels
title_full ChanFAD: A Functional Annotation Database for Ion Channels
title_fullStr ChanFAD: A Functional Annotation Database for Ion Channels
title_full_unstemmed ChanFAD: A Functional Annotation Database for Ion Channels
title_short ChanFAD: A Functional Annotation Database for Ion Channels
title_sort chanfad a functional annotation database for ion channels
topic ion channels
functional annotation
protein structure
database
proteomics
url https://www.frontiersin.org/articles/10.3389/fbinf.2022.835805/full
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