Ontology highlight
ABSTRACT:
SUBMITTER: Schmidt T
PROVIDER: S-EPMC4375483 | biostudies-literature | 2015 Mar
REPOSITORIES: biostudies-literature
Schmidt Thomas T Suk Jae-Eun JE Ye Feng F Situ Alan J AJ Mazumder Parichita P Ginsberg Mark H MH Ulmer Tobias S TS
The Journal of biological chemistry 20150129 13
Cationic membrane-proximal amino acids determine the topology of membrane proteins by interacting with anionic lipids that are restricted to the intracellular membrane leaflet. This mechanism implies that anionic lipids interfere with electrostatic interactions of membrane proteins. The integrin αIIbβ3 transmembrane (TM) complex is stabilized by a membrane-proximal αIIb(Arg(995))-β3(Asp(723)) interaction; here, we examine the influence of anionic lipids on this complex. Anionic lipids compete fo ...[more]