Role of Glycolization in Orientation of Ectodomain of Bitopic Membrane Proteins

Rog, T. (Puhuja)

Aktiviteetti: Puhe- tai esitystyypitSuullinen esitys

Kuvaus

Bitopicmembraneproteinswitha single transmembranehelix are
the largest group of membrane proteins, as approximately half of
the integral membrane proteins belong to this group. Typically
extracellular domain of bitopic proteins is heavily glycosylated.
In this study we performed molecular dynamics simulations of
three proteins: epidermal growth factor receptor (EGFR), T-cell
surface antigen CD2, and tool like receptor 4 (TLR4) in glycosylated
and non-glycosylated form. For the case of EGFR [1] and
CD2 [2] extracellular domain tends to collapse at the membrane
surface while in the presence of glycosylation upright orientation
isadopted. Thisisdueto steric effects anddueto shieldingpatches
of positively charge residues at the protein surface which fewer
interactions of proteins with lipids. For the case of TLR4 we
observed large tilting of the extracellular domain for the case of
glycosylated form of the protein in active state (with lipopolysaccharide
bound) while upright positionwas observed when carbohydrates
branches were removed.To summarize, glycosylation is
one of important determinants of the orientation of the extracellular
domains of bitopic membrane proteins.
Aikajakso27 elokuuta 20171 syyskuuta 2017
Tapahtuman otsikko 24th International Symposium on Glycoconjugates: null
Tapahtuman tyyppiKonferenssi
Sijaintijeju, Korean tasavalta (Etelä-Korea)