Details
Original language | English |
---|---|
Pages (from-to) | 93-99 |
Number of pages | 7 |
Journal | Data in Brief |
Volume | 7 |
Early online date | 13 Feb 2016 |
Publication status | Published - 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].
ASJC Scopus subject areas
Cite this
- Standard
- Harvard
- Apa
- Vancouver
- BibTeX
- RIS
In: Data in Brief, Vol. 7, 06.2016, p. 93-99.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - Data of the molecular dynamics simulations of mutations in the human connexin46 docking interface
AU - Schadzek, Patrik
AU - Schlingmann, Barbara
AU - Schaarschmidt, Frank
AU - Lindner, Julia
AU - Koval, Michael
AU - Heisterkamp, Alexander
AU - Ngezahayo, Anaclet
AU - Preller, Matthias
N1 - Funding Information: This work was supported by Transregio TR37. We are grateful to Holger Naundorf and the staff of the HLRN supercomputer for providing computational resources and support.
PY - 2016/6
Y1 - 2016/6
N2 - 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].
AB - 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].
UR - http://www.scopus.com/inward/record.url?scp=84958235820&partnerID=8YFLogxK
U2 - 10.1016/j.dib.2016.01.067
DO - 10.1016/j.dib.2016.01.067
M3 - Article
AN - SCOPUS:84958235820
VL - 7
SP - 93
EP - 99
JO - Data in Brief
JF - Data in Brief
ER -