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J Mol Biol. 2012 Jul 13;420(3):251-7. doi: 10.1016/j.jmb.2012.04.008. Epub 2012 May 4.

Homotypic interaction and amino acid distribution of unilaterally conserved transmembrane helices.

Author information

1
Lehrstuhl für Chemie der Biopolymere, Technische Universität München, Weihenstephaner Berg 3,85354 Freising, Germany.

Erratum in

  • J Mol Biol. 2012 Sep 7;422(1):161.

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.

PMID:
22561134
DOI:
10.1016/j.jmb.2012.04.008
[Indexed for MEDLINE]

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