In vivo selection of heterotypically interacting transmembrane helices: Complementary helix surfaces, rather than conserved interaction motifs, drive formation of transmembrane hetero-dimers

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• 作者：Dominik Steindorf ; Dirk Schneider ; ^{Dirk.Schneider@uni-mainz.de}
• 关键词：Transmembrane helix ; Dimerization ; Hetero-dimer ; Membrane protein ; Protein folding
• 刊名：Biochimica et Biophysica Acta (BBA) - Biomembranes
• 出版年：2017
• 出版时间：February 2017
• 年：2017
• 卷：1859
• 期：2
• 页码：245-256
• 全文大小：1423 K
• 卷排序：1859

文摘

Oligomerization of single pass TM proteins is common. A genetic screen for selecting TM hetero-dimers has been developed and applied. The architecture of TM hetero-dimers is complex and diverse. Selected amino acids and amino acid pairings nicely resemble natural TM helices. Defined motifs are not crucial for TM hetero-dimerization.