Spatial Structure of the Transmembrane Domain Heterodimer of ErbB1 and ErbB2 Receptor Tyrosine Kinases
作者： Konstantin S. Mineev , Eduard V. Bocharov , Yulia E. Pustovalova , Olga V. Bocharova , Vladimir V. Chupin
DOI: 10.1016/J.JMB.2010.05.016
关键词: Receptor tyrosine kinase 、 Biochemistry 、 Signal transduction 、 Biophysics 、 Transmembrane domain 、 Transmembrane protein 、 ErbB Receptors 、 Tyrosine kinase 、 ErbB 、 Protein structure 、 Chemistry
摘要: Growth factor receptor tyrosine kinases of the ErbB family play a significant role in vital cellular processes and various cancers. During signal transduction across plasma membrane, receptors are involved lateral homodimerization heterodimerization with proper assembly their extracellular single-span transmembrane (TM) cytoplasmic domains. The ErbB1/ErbB2 heterodimer appears to be strongest most potent inducer transformation mitogenic signaling compared other homodimers heterodimers. Spatial structure heterodimeric complex formed by TM domains ErbB1 ErbB2 embedded into lipid bicelles was obtained solution NMR. associate right-handed alpha-helical bundle through N-terminal double GG4-like motif T(648)G(649)X(2)G(652)A(653) glycine zipper T(652)X(3)S(656)X(3)G(660), respectively. described conformation is believed support juxtamembrane kinase domain configuration corresponding active state. capability for multiple polar interactions, along hydrogen bonding between segments, correlates observed highest affinity heterodimer, implying an important contribution helix-helix interaction transduction.
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