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The transmembrane domain of the oncogenic mutant ErbB-2 receptor: A structure obtained from site-specific infrared dichroism and molecular dynamics

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Beevers, Andrew J. and Kukol, Andreas (2006) The transmembrane domain of the oncogenic mutant ErbB-2 receptor: A structure obtained from site-specific infrared dichroism and molecular dynamics. Journal of Molecular Biology, Vol.361 (No.5). pp. 945-953. doi:10.1016/j.jmb.2006.07.004

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Official URL: http://dx.doi.org/10.1016/j.jmb.2006.07.004

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Abstract

ErbB-2 is a member of the family of epidermal growth factor receptors, which shows an oncogenic mutation in the rat gene neu, Val664Glu in the transmembrane domain that causes permanent dimerisation and subsequently leads to uncontrollable cell division and tumour formation. We have obtained the a-helical structure of the mutant transmembrane domain dimer experimentally with site-specific infrared dichroism (SSID) based on six transmembrane peptides with (CO)-C-13-O-18 carbonyl group-labelled residues. The derived orientational data indicate a local helix tilt ranging from 28(6) to 22(4). Altogether using orientational constraints from SSID and experimental a-helical constraints while performing a systematic conformational search including molecular dynamics simulation in a lipid bilayer, we have obtained a unique experimentally defined atomic structure. The resulting structure consists of a right handed a-helical bundle with the residues Ile659, Val663, Leu667, Ile671, Val674 and Leu679 in the dimerisation interface. The right-handed bundle is in contrast to the left-handed structures obtained in previous modelling efforts. In order to facilitate tight helical packing, the spacious Glu664 residues do not interact directly but with water molecules that enter the bilayer. (c) 2006 Elsevier Ltd. All rights reserved.

Item Type: Journal Article
Subjects: Q Science > QD Chemistry
Q Science > QH Natural history > QH301 Biology
Divisions: Faculty of Science, Engineering and Medicine > Science > Chemistry
Faculty of Science, Engineering and Medicine > Research Centres > Molecular Organisation and Assembly in Cells (MOAC)
Journal or Publication Title: Journal of Molecular Biology
Publisher: Academic Press
ISSN: 0022-2836
Official Date: 1 September 2006
Dates:
DateEvent
1 September 2006Published
Volume: Vol.361
Number: No.5
Number of Pages: 9
Page Range: pp. 945-953
DOI: 10.1016/j.jmb.2006.07.004
Status: Peer Reviewed
Publication Status: Published
Access rights to Published version: Restricted or Subscription Access

Data sourced from Thomson Reuters' Web of Knowledge

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