Homotypic interaction and amino acid distribution of unilaterally conserved transmembrane helices |
| |
| Authors: | Ried Christian Lothar Kube Sebastian Kirrbach Jan Langosch Dieter |
| |
| Institution: | 1. Department of Chemical and Geological Sciences, University of Cagliari, Cittadella Universitaria, SS 554, km 4.5, 09042, Monserrato, Cagliari, Italy;2. Neonatal Intensive Care Unit, Puericulture Institute and Neonatal Section, Azienda Ospedaliera Universitaria, University of Cagliari, SS 554, km 4.5, 09042, Monserrato, Cagliari, Italy;3. Neonatal Intensive Unit and Neonatal Pathology, “S. Giovanni Calibita” Hospital, Fatebenefratelli Isola Tiberina, Rome, Italy;4. Laboratory Medicine Service, IRCCS AOU San Martino-IST, University-Hospital, Genova, Italy |
| |
| 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. |
| |
| Keywords: | |
| 本文献已被 ScienceDirect PubMed 等数据库收录！ |
|
