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- W2108301841 endingPage "15" @default.
- W2108301841 startingPage "1" @default.
- W2108301841 abstract "Several herpes- and poxviruses have captured chemokine receptors from their hosts and modified these to their own benefit. The human and viral chemokine receptors belong to class A 7 transmembrane (TM) receptors which are characterized by several structural motifs like the DRY-motif in TM3 and the C-terminal tail. In the DRY-motif, the arginine residue serves important purposes by being directly involved in G protein coupling. Interestingly, among the viral receptors there is a greater diversity in the DRY-motif compared to their endogenous receptor homologous. The C-terminal receptor tail constitutes another regulatory region that through a number of phosphorylation sites is involved in signaling, desensitization, and internalization. Also this region is more variable among virus-encoded 7TM receptors compared to human class A receptors. In this review we will focus on these two structural motifs and discuss their role in viral 7TM receptor signaling compared to their endogenous counterparts." @default.
- W2108301841 created "2016-06-24" @default.
- W2108301841 creator A5014012202 @default.
- W2108301841 creator A5035872776 @default.
- W2108301841 creator A5039430149 @default.
- W2108301841 creator A5059116164 @default.
- W2108301841 date "2012-01-01" @default.
- W2108301841 modified "2023-10-15" @default.
- W2108301841 title "Structural Diversity in Conserved Regions Like the DRY-Motif among Viral 7TM Receptors—A Consequence of Evolutionary Pressure?" @default.
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