Homotypic interaction and amino acid distribution of unilaterally conserved transmembrane helices

Journal of Molecular Biology
Christian L RiedDieter Langosch

Abstract

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.

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Citations

Jan 30, 2013·Proceedings of the National Academy of Sciences of the United States of America·Jean-Philippe DefourStefan N Constantinescu
Aug 29, 2013·The FEBS Journal·Daniel C YeeMilton H Saier
Aug 6, 2015·Biochemistry·Mark G Teese, Dieter Langosch

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