Data of the molecular dynamics simulations of mutations in the human connexin46 docking interface

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External Research Organisations

  • Emory University
  • Hannover Medical School (MHH)
  • Deutsches Elektronen-Synchrotron (DESY)
  • Center for Systems Neuroscience Hannover (ZSN)
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Original languageEnglish
Pages (from-to)93-99
Number of pages7
JournalData in Brief
Volume7
Early online date13 Feb 2016
Publication statusPublished - Jun 2016

Abstract

The structure of hCx26 derived from the X-ray analysis was used to generate a homology model for hCx46. Interacting connexin molecules were used as starting model for the molecular dynamics (MD) simulation using NAMD and allowed us to predict the dynamic behavior of hCx46wt and the cataract related mutant hCx46N188T as well as two artificial mutants hCx46N188Q and hCx46N188D. Within the 50 ns simulation time the docked complex composed of the mutants dissociate while hCx46wt remains stable. The data indicates that one hCx46 molecule forms 5-7 hydrogen bonds (HBs) with the counterpart connexin of the opposing connexon. These HBs appear essential for a stable docking of the connexons as shown by the simulation of an entire gap junction channel and were lost for all the tested mutants. The data described here are related to the research article entitled "The cataract related mutation N188T in human connexin46 (hCx46) revealed a critical role for residue N188 in the docking process of gap junction channels" (Schadzek et al., 2015) [1].

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Data of the molecular dynamics simulations of mutations in the human connexin46 docking interface. / Schadzek, Patrik; Schlingmann, Barbara; Schaarschmidt, Frank et al.
In: Data in Brief, Vol. 7, 06.2016, p. 93-99.

Research output: Contribution to journalArticleResearchpeer review

Schadzek, P, Schlingmann, B, Schaarschmidt, F, Lindner, J, Koval, M, Heisterkamp, A, Ngezahayo, A & Preller, M 2016, 'Data of the molecular dynamics simulations of mutations in the human connexin46 docking interface', Data in Brief, vol. 7, pp. 93-99. https://doi.org/10.1016/j.dib.2016.01.067
Schadzek, P., Schlingmann, B., Schaarschmidt, F., Lindner, J., Koval, M., Heisterkamp, A., Ngezahayo, A., & Preller, M. (2016). Data of the molecular dynamics simulations of mutations in the human connexin46 docking interface. Data in Brief, 7, 93-99. https://doi.org/10.1016/j.dib.2016.01.067
Schadzek P, Schlingmann B, Schaarschmidt F, Lindner J, Koval M, Heisterkamp A et al. Data of the molecular dynamics simulations of mutations in the human connexin46 docking interface. Data in Brief. 2016 Jun;7:93-99. Epub 2016 Feb 13. doi: 10.1016/j.dib.2016.01.067
Schadzek, Patrik ; Schlingmann, Barbara ; Schaarschmidt, Frank et al. / Data of the molecular dynamics simulations of mutations in the human connexin46 docking interface. In: Data in Brief. 2016 ; Vol. 7. pp. 93-99.
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abstract = "The structure of hCx26 derived from the X-ray analysis was used to generate a homology model for hCx46. Interacting connexin molecules were used as starting model for the molecular dynamics (MD) simulation using NAMD and allowed us to predict the dynamic behavior of hCx46wt and the cataract related mutant hCx46N188T as well as two artificial mutants hCx46N188Q and hCx46N188D. Within the 50 ns simulation time the docked complex composed of the mutants dissociate while hCx46wt remains stable. The data indicates that one hCx46 molecule forms 5-7 hydrogen bonds (HBs) with the counterpart connexin of the opposing connexon. These HBs appear essential for a stable docking of the connexons as shown by the simulation of an entire gap junction channel and were lost for all the tested mutants. The data described here are related to the research article entitled {"}The cataract related mutation N188T in human connexin46 (hCx46) revealed a critical role for residue N188 in the docking process of gap junction channels{"} (Schadzek et al., 2015) [1].",
author = "Patrik Schadzek and Barbara Schlingmann and Frank Schaarschmidt and Julia Lindner and Michael Koval and Alexander Heisterkamp and Anaclet Ngezahayo and Matthias Preller",
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AU - Schadzek, Patrik

AU - Schlingmann, Barbara

AU - Schaarschmidt, Frank

AU - Lindner, Julia

AU - Koval, Michael

AU - Heisterkamp, Alexander

AU - Ngezahayo, Anaclet

AU - Preller, Matthias

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