Abstract
The high affinity IgE receptor (Fc-epsilon-RI) consists of four subunits and contains 7 transmembrane (TM) helices. Since a direct experimental structure determination of this intact receptor would be complex, a combination of computational chemistry with experimental work can be used to elucidate the 3D structure. The most suitable helix-helix packing arrangements were usually found using rules derived from soluble helical proteins and by rotating the helices such that the most hydrophobic sides would face the lipids [1]. In this work, spatial arrangement of the transmembrane bundle were studied, as well as, helix-helix interactions in the high affinity IgE receptor, using a nonsubjective procedure, namely a low resolution docking procedure [2].
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Similar content being viewed by others
References
von Heijne, G. J. Mol Biol 225, 487–494 (1992).
Vakser, I.A. Biopolymers 39, 455–464 (1996).
Zloh, M., Gibbons, W.A. Biochem. Soc. Trans. 24, 305S (1996).
Zloh, M., Esposito, D., Gibbons, W.A. Mol. Simul 24, 421–447 (2000).
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2001 Springer Science+Business Media Dordrecht
About this chapter
Cite this chapter
Zloh, M., Esposito, D., Gibbons, W.A. (2001). Docking of Transmembrane Helices Into Four Helix Bundles in the High Affinity IgE Receptor. In: Lebl, M., Houghten, R.A. (eds) Peptides: The Wave of the Future. American Peptide Symposia, vol 7. Springer, Dordrecht. https://doi.org/10.1007/978-94-010-0464-0_393
Download citation
DOI: https://doi.org/10.1007/978-94-010-0464-0_393
Publisher Name: Springer, Dordrecht
Print ISBN: 978-94-010-3905-5
Online ISBN: 978-94-010-0464-0
eBook Packages: Springer Book Archive