Contribution of charged and polar residues for the formation of the E1-E2 heterodimer from Hepatitis C Virus.

Jusoh SA, Welsch C, Siu SWI, Böckmann R, Helms V (2010)

Publication Status: Published

Publication Type: Journal article, Original article

Publication year: 2010

Journal

Journal of Molecular Modeling Springer Verlag (Germany)

Publisher: Springer Verlag (Germany)

Book Volume: 16

Pages Range: 1625-37

Volume: 16

Issue: 10

Journal Issue: 10

DOI: 10.1007/s00894-010-0672-1

Abstract

The transmembrane domains of the envelope glycoprotein E1 and E2 have crucial multifunctional roles in the biogenesis of hepatitis C virus. We have performed molecular dynamics simulations to investigate a structural model of the transmembrane segments of the E1-E2 heterodimer. The simulations support the key role of the Lys370-Asp728 ion pair for mediating the E1-E2 heterodimerization. In comparison to these two residues, the simulation results also reveal the differential effect of the conserved Arg730 residue that has been observed in experimental studies. Furthermore, we discovered the formation of inter-helical hydrogen bonds via Asn367 that stabilize dimer formation. Simulations of single and double mutants further demonstrate the importance of the ion-pair and polar interactions between the interacting helix monomers. The conformation of the E1 fragment in the simulation of the E1-E2 heterodimer is in close agreement with an NMR structure of the E1 transmembrane segment. The proposed model of the E1-E2 heterodimer supports the postulated cooperative insertion of both helices by the translocon complex into the bilayer.

Authors with CRIS profile

Shirley Weng In Siu Professur für Computational Biology Rainer Böckmann Professur für Computational Biology

Involved external institutions

Universität des Saarlandes (UdS) DE Germany (DE) Universitätsklinikum Frankfurt am Main (KGU) DE Germany (DE)

How to cite

APA:

Jusoh, S.A., Welsch, C., Siu, S.W.I., Böckmann, R., & Helms, V. (2010). Contribution of charged and polar residues for the formation of the E1-E2 heterodimer from Hepatitis C Virus. Journal of Molecular Modeling, 16(10), 1625-37. https://doi.org/10.1007/s00894-010-0672-1

MLA:

Jusoh, Siti Azma, et al. "Contribution of charged and polar residues for the formation of the E1-E2 heterodimer from Hepatitis C Virus." Journal of Molecular Modeling 16.10 (2010): 1625-37.

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