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

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Standard

Structural Diversity in Conserved Regions Like the DRY-Motif among Viral 7TM Receptors-A Consequence of Evolutionary Pressure? / Mølleskov-Jensen, Ann-Sofie; Sparre-Ulrich, Alexander Hovard; Davis-Poynter, Nicholas; Rosenkilde, Mette Marie.

I: Advances in Virology, Bind 2012, 2012, s. 231813.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Mølleskov-Jensen, A-S, Sparre-Ulrich, AH, Davis-Poynter, N & Rosenkilde, MM 2012, 'Structural Diversity in Conserved Regions Like the DRY-Motif among Viral 7TM Receptors-A Consequence of Evolutionary Pressure?', Advances in Virology, bind 2012, s. 231813. https://doi.org/10.1155/2012/231813

APA

Mølleskov-Jensen, A-S., Sparre-Ulrich, A. H., Davis-Poynter, N., & Rosenkilde, M. M. (2012). Structural Diversity in Conserved Regions Like the DRY-Motif among Viral 7TM Receptors-A Consequence of Evolutionary Pressure? Advances in Virology, 2012, 231813. https://doi.org/10.1155/2012/231813

Vancouver

Mølleskov-Jensen A-S, Sparre-Ulrich AH, Davis-Poynter N, Rosenkilde MM. Structural Diversity in Conserved Regions Like the DRY-Motif among Viral 7TM Receptors-A Consequence of Evolutionary Pressure? Advances in Virology. 2012;2012:231813. https://doi.org/10.1155/2012/231813

Author

Mølleskov-Jensen, Ann-Sofie ; Sparre-Ulrich, Alexander Hovard ; Davis-Poynter, Nicholas ; Rosenkilde, Mette Marie. / Structural Diversity in Conserved Regions Like the DRY-Motif among Viral 7TM Receptors-A Consequence of Evolutionary Pressure?. I: Advances in Virology. 2012 ; Bind 2012. s. 231813.

Bibtex

@article{53e13106d8a54425898339ecd6006dbe,
title = "Structural Diversity in Conserved Regions Like the DRY-Motif among Viral 7TM Receptors-A Consequence of Evolutionary Pressure?",
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.",
author = "Ann-Sofie M{\o}lleskov-Jensen and Sparre-Ulrich, {Alexander Hovard} and Nicholas Davis-Poynter and Rosenkilde, {Mette Marie}",
year = "2012",
doi = "10.1155/2012/231813",
language = "English",
volume = "2012",
pages = "231813",
journal = "Advances in Virology",
issn = "1687-8639",
publisher = "Hindawi Publishing Corporation",

}

RIS

TY - JOUR

T1 - Structural Diversity in Conserved Regions Like the DRY-Motif among Viral 7TM Receptors-A Consequence of Evolutionary Pressure?

AU - Mølleskov-Jensen, Ann-Sofie

AU - Sparre-Ulrich, Alexander Hovard

AU - Davis-Poynter, Nicholas

AU - Rosenkilde, Mette Marie

PY - 2012

Y1 - 2012

N2 - 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.

AB - 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.

U2 - 10.1155/2012/231813

DO - 10.1155/2012/231813

M3 - Journal article

C2 - 22899926

VL - 2012

SP - 231813

JO - Advances in Virology

JF - Advances in Virology

SN - 1687-8639

ER -

ID: 48972132