| Autor: |
Isaac K. Asare, Alberto Perez Galende, Andres Bastidas Garcia, Mateo Fernandez Cruz, Anna Clara Miranda Moura, Conner C. Campbell, Matthew Scheyer, John Paul Alao, Steve Alston, Andrea N. Kravats, Charles R. Sanders, Gary A. Lorigan, Indra D. Sahu |
| Jazyk: |
angličtina |
| Rok vydání: |
2022 |
| Předmět: |
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| Zdroj: |
Membranes, Vol 12, Iss 5, p 469 (2022) |
| Druh dokumentu: |
article |
| ISSN: |
2077-0375 |
| DOI: |
10.3390/membranes12050469 |
| Popis: |
KCNE3 is a potassium channel accessory transmembrane protein that regulates the function of various voltage-gated potassium channels such as KCNQ1. KCNE3 plays an important role in the recycling of potassium ion by binding with KCNQ1. KCNE3 can be found in the small intestine, colon, and in the human heart. Despite its biological significance, there is little information on the structural dynamics of KCNE3 in native-like membrane environments. Molecular dynamics (MD) simulations are a widely used as a tool to study the conformational dynamics and interactions of proteins with lipid membranes. In this study, we have utilized all-atom molecular dynamics simulations to characterize the molecular motions and the interactions of KCNE3 in a bilayer composed of: a mixture of POPC and POPG lipids (3:1), POPC alone, and DMPC alone. Our MD simulation results suggested that the transmembrane domain (TMD) of KCNE3 is less flexible and more stable when compared to the N- and C-termini of KCNE3 in all three membrane environments. The conformational flexibility of N- and C-termini varies across these three lipid environments. The MD simulation results further suggested that the TMD of KCNE3 spans the membrane width, having residue A69 close to the center of the lipid bilayers and residues S57 and S82 close to the lipid bilayer membrane surfaces. These results are consistent with previous biophysical studies of KCNE3. The outcomes of these MD simulations will help design biophysical experiments and complement the experimental data obtained on KCNE3 to obtain a more detailed understanding of its structural dynamics in the native membrane environment. |
| Databáze: |
Directory of Open Access Journals |
| Externí odkaz: |
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