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

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...

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Bibliographic Details
Published in:Advances in virology 2012-01, Vol.2012 (2012), p.1-15
Main Authors: Rosenkilde, Mette Marie, Davis-Poynter, Nicholas, Sparre-Ulrich, Alexander Hovard, Jensen, Ann-Sofie Mølleskov
Format: Article
Language:English
Subjects:
Chemokines
Colleges & universities
Crystal structure
Kinases
Ligands
Pharmacology
Proteins
Review
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Summary: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.
ISSN:1687-8639
1687-8647
DOI:10.1155/2012/231813