AI Article Synopsis
- Proper dimerization of receptor tyrosine kinases' transmembrane domains is essential for signaling across the plasma membrane.
- The spatial structure of the ErbB2 receptor's transmembrane domain was studied using solution NMR and molecular dynamics in a lipid environment.
- The interaction of ErbB2 segments forms a right-handed alpha-helical structure, with a specific motif that explains the effects of certain mutations associated with cancer.
Article Abstract
Proper lateral dimerization of the transmembrane domains of receptor tyrosine kinases is required for biochemical signal transduction across the plasma membrane. The spatial structure of the dimeric transmembrane domain of the growth factor receptor ErbB2 embedded into lipid bicelles was obtained by solution NMR, followed by molecular dynamics relaxation in an explicit lipid bilayer. ErbB2 transmembrane segments associate in a right-handed alpha-helical bundle through the N-terminal tandem GG4-like motif Thr652-X3-Ser656-X3-Gly660, providing an explanation for the pathogenic power of some oncogenic mutations.
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| http://dx.doi.org/10.1074/jbc.M709202200 | DOI Listing |
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