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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| Format: | Article |
| Language: | English |
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Wiley
2012-01-01
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| Series: | Advances in Virology |
| Online Access: | http://dx.doi.org/10.1155/2012/231813 |
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| author | Ann-Sofie Mølleskov Jensen Alexander Hovard Sparre-Ulrich Nicholas Davis-Poynter Mette Marie Rosenkilde |
| author_facet | Ann-Sofie Mølleskov Jensen Alexander Hovard Sparre-Ulrich Nicholas Davis-Poynter Mette Marie Rosenkilde |
| author_sort | Ann-Sofie Mølleskov Jensen |
| collection | DOAJ |
| description | 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. |
| format | Article |
| id | doaj-art-eebf50ec638742a4ad3f41febfa8a9fa |
| institution | DOAJ |
| issn | 1687-8639 1687-8647 |
| language | English |
| publishDate | 2012-01-01 |
| publisher | Wiley |
| record_format | Article |
| series | Advances in Virology |
| spelling | doaj-art-eebf50ec638742a4ad3f41febfa8a9fa2025-08-20T03:21:13ZengWileyAdvances in Virology1687-86391687-86472012-01-01201210.1155/2012/231813231813Structural Diversity in Conserved Regions Like the DRY-Motif among Viral 7TM Receptors—A Consequence of Evolutionary Pressure?Ann-Sofie Mølleskov Jensen0Alexander Hovard Sparre-Ulrich1Nicholas Davis-Poynter2Mette Marie Rosenkilde3Laboratory for Molecular Pharmacology, Department of Neuroscience and Pharmacology, The Panum Institute, University of Copenhagen, Building 18.5, Blegdamsvej 3, 2200-Copenhagen N, DenmarkLaboratory for Molecular Pharmacology, Department of Neuroscience and Pharmacology, The Panum Institute, University of Copenhagen, Building 18.5, Blegdamsvej 3, 2200-Copenhagen N, DenmarkSir Albert Sakzewski Virus Research Centre (SASVRC), Royal Children's Hospital/Clinical Medical Virology Centre (CMVC), University of Queensland, St Lucia, QLD 4072, AustraliaLaboratory for Molecular Pharmacology, Department of Neuroscience and Pharmacology, The Panum Institute, University of Copenhagen, Building 18.5, Blegdamsvej 3, 2200-Copenhagen N, DenmarkSeveral 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.http://dx.doi.org/10.1155/2012/231813 |
| spellingShingle | Ann-Sofie Mølleskov Jensen Alexander Hovard Sparre-Ulrich Nicholas Davis-Poynter Mette Marie Rosenkilde Structural Diversity in Conserved Regions Like the DRY-Motif among Viral 7TM Receptors—A Consequence of Evolutionary Pressure? Advances in Virology |
| title | Structural Diversity in Conserved Regions Like the DRY-Motif among Viral 7TM Receptors—A Consequence of Evolutionary Pressure? |
| title_full | Structural Diversity in Conserved Regions Like the DRY-Motif among Viral 7TM Receptors—A Consequence of Evolutionary Pressure? |
| title_fullStr | Structural Diversity in Conserved Regions Like the DRY-Motif among Viral 7TM Receptors—A Consequence of Evolutionary Pressure? |
| title_full_unstemmed | Structural Diversity in Conserved Regions Like the DRY-Motif among Viral 7TM Receptors—A Consequence of Evolutionary Pressure? |
| title_short | Structural Diversity in Conserved Regions Like the DRY-Motif among Viral 7TM Receptors—A Consequence of Evolutionary Pressure? |
| title_sort | structural diversity in conserved regions like the dry motif among viral 7tm receptors a consequence of evolutionary pressure |
| url | http://dx.doi.org/10.1155/2012/231813 |
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