Structural biology of chemokine receptors

Chemokine receptors are G protein-coupled receptors that mediate migration and activation of leukocytes as an important part of a protective immune response to injury and infection. In addition, chemokine receptors are used by HIV-1 to infect CD4 positive cells. The structural bases of chemokine rec...

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Autores principales:	ROJO,DANIEL, SUETOMI,KATSUTOSHI, NAVARRO,JAVIER
Lenguaje:	English
Publicado:	Sociedad de Biología de Chile 1999
Materias:	Chemokines G-protein coupled receptors Inflammation HIV-1
Acceso en línea:	http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0716-97601999000400006
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spelling	oai:scielo:S0716-976019990004000062000-11-27Structural biology of chemokine receptorsROJO,DANIELSUETOMI,KATSUTOSHINAVARRO,JAVIER Chemokines G-protein coupled receptors Inflammation HIV-1 Chemokine receptors are G protein-coupled receptors that mediate migration and activation of leukocytes as an important part of a protective immune response to injury and infection. In addition, chemokine receptors are used by HIV-1 to infect CD4 positive cells. The structural bases of chemokine receptor recognition and signal transduction are currently being investigated. High-resolution X-ray diffraction and NMR spectroscopy of chemokines indicate that all these peptides exhibit a common folding pattern, in spite of its low degree of primary-sequence homology. Chemokines' functional motifs have been identified by mutagenesis studies, and a possible mechanism for receptor recognition and activation is proposed, but high-resolution structure data of chemokine receptors is not yet available. Studies with receptor chimeras have identified the putative extracellular domains as the major selectivity determinants. Single-amino acid substitutions in the extracellular domains produce profound changes in receptor specificity, suggesting that motifs in these domains operate as a restrictive barrier to a common activation motif. Similarly HIV-1 usage of chemokine receptors involves interaction of one or more extracellular domains of the receptor with conserved and variable domains on the viral envelope protein gp 120, indicating a highly complex interaction. Elucidating the structural requirements for receptor interaction with chemokines and with HIV-1 will provide important insights into understanding the mechanisms of chemokine recognition and receptor activation. In addition, this information can greatly facilitate the design of effective inmunomodulatory and anti-HIV-1 therapeutic agentsinfo:eu-repo/semantics/openAccessSociedad de Biología de ChileBiological Research v.32 n.4 19991999-01-01text/htmlhttp://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0716-97601999000400006en10.4067/S0716-97601999000400006
institution	Scielo Chile
collection	Scielo Chile
language	English
topic	Chemokines G-protein coupled receptors Inflammation HIV-1
spellingShingle	Chemokines G-protein coupled receptors Inflammation HIV-1 ROJO,DANIEL SUETOMI,KATSUTOSHI NAVARRO,JAVIER Structural biology of chemokine receptors
description	Chemokine receptors are G protein-coupled receptors that mediate migration and activation of leukocytes as an important part of a protective immune response to injury and infection. In addition, chemokine receptors are used by HIV-1 to infect CD4 positive cells. The structural bases of chemokine receptor recognition and signal transduction are currently being investigated. High-resolution X-ray diffraction and NMR spectroscopy of chemokines indicate that all these peptides exhibit a common folding pattern, in spite of its low degree of primary-sequence homology. Chemokines' functional motifs have been identified by mutagenesis studies, and a possible mechanism for receptor recognition and activation is proposed, but high-resolution structure data of chemokine receptors is not yet available. Studies with receptor chimeras have identified the putative extracellular domains as the major selectivity determinants. Single-amino acid substitutions in the extracellular domains produce profound changes in receptor specificity, suggesting that motifs in these domains operate as a restrictive barrier to a common activation motif. Similarly HIV-1 usage of chemokine receptors involves interaction of one or more extracellular domains of the receptor with conserved and variable domains on the viral envelope protein gp 120, indicating a highly complex interaction. Elucidating the structural requirements for receptor interaction with chemokines and with HIV-1 will provide important insights into understanding the mechanisms of chemokine recognition and receptor activation. In addition, this information can greatly facilitate the design of effective inmunomodulatory and anti-HIV-1 therapeutic agents
author	ROJO,DANIEL SUETOMI,KATSUTOSHI NAVARRO,JAVIER
author_facet	ROJO,DANIEL SUETOMI,KATSUTOSHI NAVARRO,JAVIER
author_sort	ROJO,DANIEL
title	Structural biology of chemokine receptors
title_short	Structural biology of chemokine receptors
title_full	Structural biology of chemokine receptors
title_fullStr	Structural biology of chemokine receptors
title_full_unstemmed	Structural biology of chemokine receptors
title_sort	structural biology of chemokine receptors
publisher	Sociedad de Biología de Chile
publishDate	1999
url	http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0716-97601999000400006
work_keys_str_mv	AT rojodaniel structuralbiologyofchemokinereceptors AT suetomikatsutoshi structuralbiologyofchemokinereceptors AT navarrojavier structuralbiologyofchemokinereceptors
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Structural biology of chemokine receptors

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