Evolutionary, structural and functional interplay of the IκB family members.

A primary level of control for nuclear factor kappa B (NF-κB) is effected through its interactions with the inhibitor protein, inhibitor of kappa B (IκB). Several lines of evidence confirm the existence of multiple forms of IκB that appear to regulate NF-κB by distinct mechanisms. Therefore, we perf...

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Autores principales:	Shaherin Basith, Balachandran Manavalan, Vijayakumar Gosu, Sangdun Choi
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2013
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/15969a54fe8f4dec8a05d49fbd7b65d4
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spelling	oai:doaj.org-article:15969a54fe8f4dec8a05d49fbd7b65d42021-11-18T08:00:19ZEvolutionary, structural and functional interplay of the IκB family members.1932-620310.1371/journal.pone.0054178https://doaj.org/article/15969a54fe8f4dec8a05d49fbd7b65d42013-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23372681/?tool=EBIhttps://doaj.org/toc/1932-6203A primary level of control for nuclear factor kappa B (NF-κB) is effected through its interactions with the inhibitor protein, inhibitor of kappa B (IκB). Several lines of evidence confirm the existence of multiple forms of IκB that appear to regulate NF-κB by distinct mechanisms. Therefore, we performed a comprehensive bioinformatics analysis to understand the evolutionary history and intrinsic functional diversity of IκB family members. Phylogenetic relationships were constructed to trace the evolution of the IκB family genes. Our phylogenetic analysis revealed 10 IκB subfamily members that clustered into 5 major clades. Since the ankyrin (ANK) domain appears to be more ancient than the Rel homology domain (RHD), our phylogenetic analysis suggests that some undefined ancestral set of ANK repeats acquired an RHD before any duplication and was later duplicated and then diverged into the different IκB subfamilies. Functional analysis identified several functionally divergent sites in the ANK repeat domains (ARDs) and revealed that this region has undergone strong purifying selection, suggesting its functional importance in IκB genes. Structural analysis showed that the major variations in the number of ANK repeats and high conformational changes in the finger loop ARD region contribute to the differing binding partner specificities, thereby leading to distinct IκB functions. In summary, our study has provided useful information about the phylogeny and structural and functional divergence of the IκB family. Additionally, we identified a number of amino acid sites that contribute to the predicted functional divergence of these proteins.Shaherin BasithBalachandran ManavalanVijayakumar GosuSangdun ChoiPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 8, Iss 1, p e54178 (2013)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Shaherin Basith Balachandran Manavalan Vijayakumar Gosu Sangdun Choi Evolutionary, structural and functional interplay of the IκB family members.
description	A primary level of control for nuclear factor kappa B (NF-κB) is effected through its interactions with the inhibitor protein, inhibitor of kappa B (IκB). Several lines of evidence confirm the existence of multiple forms of IκB that appear to regulate NF-κB by distinct mechanisms. Therefore, we performed a comprehensive bioinformatics analysis to understand the evolutionary history and intrinsic functional diversity of IκB family members. Phylogenetic relationships were constructed to trace the evolution of the IκB family genes. Our phylogenetic analysis revealed 10 IκB subfamily members that clustered into 5 major clades. Since the ankyrin (ANK) domain appears to be more ancient than the Rel homology domain (RHD), our phylogenetic analysis suggests that some undefined ancestral set of ANK repeats acquired an RHD before any duplication and was later duplicated and then diverged into the different IκB subfamilies. Functional analysis identified several functionally divergent sites in the ANK repeat domains (ARDs) and revealed that this region has undergone strong purifying selection, suggesting its functional importance in IκB genes. Structural analysis showed that the major variations in the number of ANK repeats and high conformational changes in the finger loop ARD region contribute to the differing binding partner specificities, thereby leading to distinct IκB functions. In summary, our study has provided useful information about the phylogeny and structural and functional divergence of the IκB family. Additionally, we identified a number of amino acid sites that contribute to the predicted functional divergence of these proteins.
format	article
author	Shaherin Basith Balachandran Manavalan Vijayakumar Gosu Sangdun Choi
author_facet	Shaherin Basith Balachandran Manavalan Vijayakumar Gosu Sangdun Choi
author_sort	Shaherin Basith
title	Evolutionary, structural and functional interplay of the IκB family members.
title_short	Evolutionary, structural and functional interplay of the IκB family members.
title_full	Evolutionary, structural and functional interplay of the IκB family members.
title_fullStr	Evolutionary, structural and functional interplay of the IκB family members.
title_full_unstemmed	Evolutionary, structural and functional interplay of the IκB family members.
title_sort	evolutionary, structural and functional interplay of the iκb family members.
publisher	Public Library of Science (PLoS)
publishDate	2013
url	https://doaj.org/article/15969a54fe8f4dec8a05d49fbd7b65d4
work_keys_str_mv	AT shaherinbasith evolutionarystructuralandfunctionalinterplayoftheikbfamilymembers AT balachandranmanavalan evolutionarystructuralandfunctionalinterplayoftheikbfamilymembers AT vijayakumargosu evolutionarystructuralandfunctionalinterplayoftheikbfamilymembers AT sangdunchoi evolutionarystructuralandfunctionalinterplayoftheikbfamilymembers
_version_	1718422650635681792

Evolutionary, structural and functional interplay of the IκB family members.

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