Coils in the membrane core are conserved and functionally important
2008 (English)In: Journal of Molecular Biology, ISSN 0022-2836, Vol. 380, no 1, 170-180 p.Article in journal (Refereed) Published
With the increasing number of available α-helical transmembrane (TM) protein structures, the traditional picture of membrane proteins has been challenged. For example, reentrant regions, which enter and exit the membrane at the same side, and interface helices, which lie parallel with the membrane in the membrane–water interface, are common. Furthermore, TM helices are frequently kinked, and their length and tilt angle vary. Here, we systematically analyze 7% of all residues within the deep membrane core that are in coil state. These coils can be found in TM-helix kinks as major breaks in TM helices and as parts of reentrant regions.
Coil residues are significantly more conserved than other residues. Due to the polar character of the coil backbone, they are either buried or located near aqueous channels. Coil residues are frequently found within channels and transporters, where they introduce the flexibility and polarity required for transport across the membrane. Therefore, we believe that coil residues in the membrane core, while constituting a structural anomaly, are essential for the function of proteins.
Place, publisher, year, edition, pages
2008. Vol. 380, no 1, 170-180 p.
Amino Acid Sequence, Amino Acid Substitution, Conserved Sequence, Hydrogen Bonding, Ion Channels/chemistry, Membrane Proteins/*chemistry/*metabolism, Membrane Transport Proteins/chemistry, Models; Molecular, Protein Structure; Secondary, Software, Structure-Activity Relationship
IdentifiersURN: urn:nbn:se:su:diva-14856DOI: 10.1016/j.jmb.2008.04.052ISI: 000257469600014PubMedID: 18511074OAI: oai:DiVA.org:su-14856DiVA: diva2:181376