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Adv Virol. 2012; 2012: 231813.
Published online Jul 30, 2012. doi:  10.1155/2012/231813
PMCID: PMC3414077
Structural Diversity in Conserved Regions Like the DRY-Motif among Viral 7TM Receptors—A Consequence of Evolutionary Pressure?
Ann-Sofie Mølleskov Jensen, 1 Alexander Hovard Sparre-Ulrich, 1 Nicholas Davis-Poynter, 2 and Mette Marie Rosenkilde 1 *
1Laboratory for Molecular Pharmacology, Department of Neuroscience and Pharmacology, The Panum Institute, University of Copenhagen, Building 18.5, Blegdamsvej 3, 2200-Copenhagen N, Denmark
2Sir Albert Sakzewski Virus Research Centre (SASVRC), Royal Children's Hospital/Clinical Medical Virology Centre (CMVC), University of Queensland, St Lucia, QLD 4072, Australia
*Mette Marie Rosenkilde: rosenkilde/at/sund.ku.dk
Academic Editor: Rika Draenert
Received March 15, 2012; Accepted May 31, 2012.
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.
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