Structural Diversity in Conserved Regions Like the DRY-Motif among Viral 7TM Receptors—A Consequence of Evolutionary Pressure?

الملخص EN

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.