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.

journal_name

Biochemistry

journal_title

Biochemistry

authors

Ried CL,Scharnagl C,Langosch D

doi

10.1021/acs.biochem.5b01239

subject

Has Abstract

pub_date

2016-03-08 00:00:00

pages

1287-90

issue

9

eissn

0006-2960

issn

1520-4995

journal_volume

55

pub_type

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