Article
Transmembrane helix orientation influences membrane binding of the intracellular juxtamembrane domain in Neu receptor peptides.
Proceedings of the National Academy of Sciences of the United States of America - 29 Jan 2013
Matsushita Chihiro, Tamagaki Hiroko, Miyazawa Yudai, Aimoto Saburo, Smith Steven O, Sato Takeshi
Abstract excerpt
The transmembrane (TM) and juxtamembrane (JM) regions of the ErbB family receptor tyrosine kinases connect the extracellular ligand-binding domain to the intracellular kinase domain. Evidence for the role of these regions in the mechanism of receptor dimerization and activation is provided by TM-JM peptides corresponding to the Neu (or rat ErbB2) receptor. Solid-state NMR and fluorescence spectroscopy show that...
Topics
- Amino Acid Sequence
- Amino Acid Substitution
- Animals
- Calmodulin
- Kinetics
- Lipid Bilayers
- Magnetic Resonance Spectroscopy
- Membrane Proteins
- Molecular Sequence Data
- Mutation
- Peptides
- Protein Binding
- Protein Multimerization