Homotypic Interaction and Amino Acid Distribution of Unilaterally Conserved Transmembrane Helices

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• 作者：Christian Lothar Ried ; Sebastian Kube¹ ; Jan Kirrbach ; Dieter Langosch ; ^{langosch@tum.de}
• 关键词：TMD ; transmembrane domain ; CM ; conservation moment ; SIMAP ; Similarity Matrix of Proteins ; GpA ; glycophorin A
• 刊名：Journal of Molecular Biology
• 出版年：2012
• 期刊代码：102_00222836
• 类别：imm
• 出版时间：13 July, 2012
• 卷：420
• 期：3
• 页码：251-257
• 文件大小：480 K

摘要

Formation of non-covalent functional complexes of integral membrane proteins is frequently supported by sequence-specific interaction of their transmembrane helices. Here, we aligned human single-span membrane proteins with orthologs from other eukaryotes. We find that almost half of the human single-span membrane proteins contain a transmembrane helix that exhibits significant non-random unilateral conservation. Furthermore, unilateral conservation of transmembrane domains (TMDs) correlates well with their ability to self-interact. Glycine, polar non-ionizable, and aromatic amino acids are overrepresented in conserved versus non-conserved helix faces. Hence, our genome-wide analysis indicates that these amino acid types generally support interaction of single-span membrane protein TMDs.