The mechanism of complex formation between calmodulin and voltage gated calcium channels revealed by molecular dynamics.

Calmodulin, a ubiquitous eukaryotic calcium sensor responsible for the regulation of many fundamental cellular processes, is a highly flexible protein and exhibits an unusually wide range of conformations. Furthermore, CaM is known to interact with more than 300 cellular targets. Molecular dynamics...

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Autores principales:	Shivani Yaduvanshi, Rya Ero, Veerendra Kumar
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2021
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/d65587789a5045ccaa66e990323555dd
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spelling	oai:doaj.org-article:d65587789a5045ccaa66e990323555dd2021-12-02T20:17:21ZThe mechanism of complex formation between calmodulin and voltage gated calcium channels revealed by molecular dynamics.1932-620310.1371/journal.pone.0258112https://doaj.org/article/d65587789a5045ccaa66e990323555dd2021-01-01T00:00:00Zhttps://doi.org/10.1371/journal.pone.0258112https://doaj.org/toc/1932-6203Calmodulin, a ubiquitous eukaryotic calcium sensor responsible for the regulation of many fundamental cellular processes, is a highly flexible protein and exhibits an unusually wide range of conformations. Furthermore, CaM is known to interact with more than 300 cellular targets. Molecular dynamics (MD) simulation trajectories suggest that EF-hand loops show different magnitudes of flexibility. Therefore, the four EF-hand motifs have different affinities for Ca2+ ions, which enables CaM to function on wide range of Ca2+ ion concentrations. EF-hand loops are 2-3 times more flexible in apo CaM whereas least flexible in Ca2+/CaM-IQ motif complexes. We report a unique intermediate conformation of Ca2+/CaM while transitioning from extended to compact form. We also report the complex formation process between Ca2+/CaM and IQ CaM-binding motifs. Our results showed how IQ motif recognise its binding site on the CaM and how CaM transforms from extended to compact form upon binding to IQ motif.Shivani YaduvanshiRya EroVeerendra KumarPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 16, Iss 10, p e0258112 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Shivani Yaduvanshi Rya Ero Veerendra Kumar The mechanism of complex formation between calmodulin and voltage gated calcium channels revealed by molecular dynamics.
description	Calmodulin, a ubiquitous eukaryotic calcium sensor responsible for the regulation of many fundamental cellular processes, is a highly flexible protein and exhibits an unusually wide range of conformations. Furthermore, CaM is known to interact with more than 300 cellular targets. Molecular dynamics (MD) simulation trajectories suggest that EF-hand loops show different magnitudes of flexibility. Therefore, the four EF-hand motifs have different affinities for Ca2+ ions, which enables CaM to function on wide range of Ca2+ ion concentrations. EF-hand loops are 2-3 times more flexible in apo CaM whereas least flexible in Ca2+/CaM-IQ motif complexes. We report a unique intermediate conformation of Ca2+/CaM while transitioning from extended to compact form. We also report the complex formation process between Ca2+/CaM and IQ CaM-binding motifs. Our results showed how IQ motif recognise its binding site on the CaM and how CaM transforms from extended to compact form upon binding to IQ motif.
format	article
author	Shivani Yaduvanshi Rya Ero Veerendra Kumar
author_facet	Shivani Yaduvanshi Rya Ero Veerendra Kumar
author_sort	Shivani Yaduvanshi
title	The mechanism of complex formation between calmodulin and voltage gated calcium channels revealed by molecular dynamics.
title_short	The mechanism of complex formation between calmodulin and voltage gated calcium channels revealed by molecular dynamics.
title_full	The mechanism of complex formation between calmodulin and voltage gated calcium channels revealed by molecular dynamics.
title_fullStr	The mechanism of complex formation between calmodulin and voltage gated calcium channels revealed by molecular dynamics.
title_full_unstemmed	The mechanism of complex formation between calmodulin and voltage gated calcium channels revealed by molecular dynamics.
title_sort	mechanism of complex formation between calmodulin and voltage gated calcium channels revealed by molecular dynamics.
publisher	Public Library of Science (PLoS)
publishDate	2021
url	https://doaj.org/article/d65587789a5045ccaa66e990323555dd
work_keys_str_mv	AT shivaniyaduvanshi themechanismofcomplexformationbetweencalmodulinandvoltagegatedcalciumchannelsrevealedbymoleculardynamics AT ryaero themechanismofcomplexformationbetweencalmodulinandvoltagegatedcalciumchannelsrevealedbymoleculardynamics AT veerendrakumar themechanismofcomplexformationbetweencalmodulinandvoltagegatedcalciumchannelsrevealedbymoleculardynamics AT shivaniyaduvanshi mechanismofcomplexformationbetweencalmodulinandvoltagegatedcalciumchannelsrevealedbymoleculardynamics AT ryaero mechanismofcomplexformationbetweencalmodulinandvoltagegatedcalciumchannelsrevealedbymoleculardynamics AT veerendrakumar mechanismofcomplexformationbetweencalmodulinandvoltagegatedcalciumchannelsrevealedbymoleculardynamics
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The mechanism of complex formation between calmodulin and voltage gated calcium channels revealed by molecular dynamics.

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