title: Entrapment of Water at the Transmembrane Helix-Helix Interface of Quiescin Sulfhydryl Oxidase 2.
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.
authors.affiliation: Lehrstuhl Chemie der Biopolymere, Technische Universität München , Weihenstephaner Berg 3, 85354 Freising, and Munich Center For Integrated Protein Science (CIPSM), Germany.
authors.forename: Christian L
authors.initials: CL
authors.lastname: Ried
authors.affiliation: Fakultät für Physik E14, Technische Universität München , Maximus-von-Imhof-Forum 4, 85354 Freising, Germany.
authors.forename: Christina
authors.initials: C
authors.lastname: Scharnagl
authors.affiliation: Lehrstuhl Chemie der Biopolymere, Technische Universität München , Weihenstephaner Berg 3, 85354 Freising, and Munich Center For Integrated Protein Science (CIPSM), Germany.
authors.forename: Dieter
authors.initials: D
authors.lastname: Langosch
mesh_terms: D000595:Amino Acid Sequence; D002462:Cell Membrane / Q000235:genetics / Q000378:metabolism; D018257:Helix-Loop-Helix Motifs / Q000502:physiology*; D006801:Humans; D008969:Molecular Sequence Data; D050862:Oxidoreductases Acting on Sulfur Group Donors / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D017433:Protein Structure, Secondary; D014867:Water / Q000378:metabolism*
chemical_list: D014867:Water; D050862:Oxidoreductases Acting on Sulfur Group Donors; C481160:QSOX2 protein, human