Parametrisation of the free energy of ATP binding to wild-type and mutant Kir6.2 potassium channels

Morán, Óscar; Grottesi, Alessandro; Chadburn, Andrew J.; Tammaro, Paolo

doi:10.1016/j.bpc.2012.10.006

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Atp Binding Free Energy1

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Cited by 2 publications

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“…Table 4 shows the van der Waals and electrostatic energy term contributions and the differences between the free and bound ATP calculated for WT and mutant CFTR. Because the lack of enough experimental data to parametrize the LIE analysis [32], we used the parameters a ¼ 0.183, b ¼ 0.43 and g ¼ 0, as proposed by the group of Aqvist [33,34]. In these conditions, it becomes difficult to evaluate the absolute value of the DG bind .…”

Section: Atp Binding Free Energymentioning

confidence: 99%

On the interactions between nucleotide binding domains and membrane spanning domains in cystic fibrosis transmembrane regulator: A molecular dynamic study

Belmonte

Morán

2015

Biochimie

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Section: Atp Binding Free Energymentioning

confidence: 99%

On the interactions between nucleotide binding domains and membrane spanning domains in cystic fibrosis transmembrane regulator: A molecular dynamic study

Belmonte

Morán

2015

Biochimie

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Insights into channel dysfunction from modelling and molecular dynamics simulations

et al. 2018

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Developments in structural biology mean that the number of different ion channel structures has increased significantly in recent years. Structures of ion channels enable us to rationalize how mutations may lead to channelopathies. However, determining the structures of ion channels is still not trivial, especially as they necessarily exist in many distinct functional states. Therefore, the use of computational modelling can provide complementary information that can refine working hypotheses of both wild type and mutant ion channels. The simplest but still powerful tool is homology modelling. Many structures are available now that can provide suitable templates for many different types of ion channels, allowing a full three-dimensional interpretation of mutational effects. These structural models, and indeed the structures themselves obtained by X-ray crystallography, and more recently cryo-electron microscopy, can be subjected to molecular dynamics simulations, either as a tool to help explore the conformational dynamics in detail or simply as a means to refine the models further. Here we review how these approaches have been used to improve our understanding of how diseases might be linked to specific mutations in ion channel proteins. This article is part of the Special Issue entitled 'Channelopathies.'

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Parametrisation of the free energy of ATP binding to wild-type and mutant Kir6.2 potassium channels

Cited by 2 publications

References 58 publications

On the interactions between nucleotide binding domains and membrane spanning domains in cystic fibrosis transmembrane regulator: A molecular dynamic study

On the interactions between nucleotide binding domains and membrane spanning domains in cystic fibrosis transmembrane regulator: A molecular dynamic study

Insights into channel dysfunction from modelling and molecular dynamics simulations

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