Membranes & Sorting | Virology | Membrane Proteins & Energy Transduction | Theory & Simulation | Structural Genomics
How do marginally hydrophobic TM domains behave in lipid bilayer?
Siti Azma Jusoh*, Volkhard Helms
*Corresponding author: Siti Azma Jusoh
Lehrstuhl für Computational Biology, Universität des Saarlandes, Saarbrücken, Germany
Faculty of Pharmacy, Universiti Teknologi MARA, Selangor, Malaysia
F1000Posters 2011, 2: 97 (poster) [ENGLISH]
Poster [4.38 MB]
Presented at
Biochemical Society 2011 - Annual Symposium - Recent Advances in Membrane Biochemistry,
5 - 7 Jan 2011, P115
The putative transmembrane domains ™ of the envelope glycoproteins from the family Flaviviridae consist of a highly polar segment in between two hydrophobic stretches. The mutagenesis studies by the Dubuisson group have shown that the TM domains not only act as a membrane anchor, but are also responsible for the heterodimerization as signal anchors.
We observed in the simulations that these marginally hydrophobic segments from hepatitis C (HCV), dengue, Japanese encephalitis, West Nile and bovine viral diarrhea viruses showed a similar structural behaviour when they were placed as isolated helices in a membrane lipid bilayer. The TM domains of the E1/prM tended to tilt and remain helical during 200 ns MD simulations. In contrast, the TM domains of the E2/E that contain a central Asp residue were severely kinked.
For HCV, the TM domains of E1 and E2 were hypothesized to heterodimerize via an ion pair of Lys-Asp amino acids. We showed that the HCV: E1-E2 heterodimer formed by the charged residues located in the core region of the membrane lipid bilayer stabilized the helical conformation of E2 compared to E2 existing as a single-pass TM helix. This work provides new insight into the interaction between integral membrane proteins and the lipid bilayer.
No relevant conflicts of interest declared.
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