Abstract:
:Little is known about how a membrane can regulate interactions between transmembrane helices. Here, we show that strong self-interaction of the transmembrane helix of human quiescin sulfhydryl oxidase 2 rests on a motif of conserved amino acids comprising one face of the helix. Atomistic molecular dynamics simulations suggest that water molecules enter the helix-helix interface and connect serine residues of both partner helices. In addition, an interfacial tyrosine can interact with noninterfacial water or lipid. Dimerization of this transmembrane helix might therefore be controlled by membrane properties controlling water permeation and/or by the lipid composition of the membrane.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Ried CL,Scharnagl C,Langosch Ddoi
10.1021/acs.biochem.5b01239subject
Has Abstractpub_date
2016-03-08 00:00:00pages
1287-90issue
9eissn
0006-2960issn
1520-4995journal_volume
55pub_type
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