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对DARC跨膜蛋白结构模型的多种研究兴趣。

Multiple interests in structural models of DARC transmembrane protein.

作者信息

Smolarek D, Bertrand O, Czerwinski M, Colin Y, Etchebest C, de Brevern A G

机构信息

Inserm UMR-S 665, dynamique des structures et interactions des macromolecules biologiques (DSIMB), 6, rue Alexandre-Cabanel, 75739 Paris cedex 15, France.

出版信息

Transfus Clin Biol. 2010 Sep;17(3):184-96. doi: 10.1016/j.tracli.2010.05.003. Epub 2010 Jul 23.

DOI:10.1016/j.tracli.2010.05.003
PMID:20655787
Abstract

Duffy Antigen Receptor for Chemokines (DARC) is an unusual transmembrane chemokine receptor which (i) binds the two main chemokine families and (ii) does not transduct any signal as it lacks the DRY consensus sequence. It is considered as silent chemokine receptor, a tank useful for chemiotactism. DARC had been particularly studied as a major actor of malaria infection by Plasmodium vivax. It is also implicated in multiple chemokine inflammation, inflammatory diseases, in cancer and might play a role in HIV infection and AIDS. In this review, we focus on the interest to build structural model of DARC to understand more precisely its abilities to bind its physiological ligand CXCL8 and its malaria ligand. We also present innovative development on VHHs able to bind DARC protein. We underline difficulties and limitations of such bioinformatics approaches and highlight the crucial importance of biological data to conduct these kinds of researches.

摘要

趋化因子的达菲抗原受体(DARC)是一种不同寻常的跨膜趋化因子受体,它(i)结合两个主要的趋化因子家族,并且(ii)由于缺乏DRY共有序列而不传导任何信号。它被认为是沉默趋化因子受体,是一种用于趋化作用的“容器”。DARC作为间日疟原虫疟疾感染的主要作用因子受到了特别研究。它还与多种趋化因子炎症、炎症性疾病、癌症有关,并且可能在HIV感染和艾滋病中发挥作用。在这篇综述中,我们聚焦于构建DARC结构模型以更精确地了解其结合生理配体CXCL8和疟疾配体能力的意义。我们还展示了能够结合DARC蛋白的VHHs的创新性进展。我们强调了此类生物信息学方法的困难和局限性,并突出了生物学数据对开展这类研究的至关重要性。

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1
Multiple interests in structural models of DARC transmembrane protein.对DARC跨膜蛋白结构模型的多种研究兴趣。
Transfus Clin Biol. 2010 Sep;17(3):184-96. doi: 10.1016/j.tracli.2010.05.003. Epub 2010 Jul 23.
2
A structural model of a seven-transmembrane helix receptor: the Duffy antigen/receptor for chemokine (DARC).一种七跨膜螺旋受体的结构模型:趋化因子的达菲抗原/受体(DARC)。
Biochim Biophys Acta. 2005 Aug 5;1724(3):288-306. doi: 10.1016/j.bbagen.2005.05.016.
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In silico studies on DARC.关于趋化因子Duffy抗原/趋化因子受体(DARC)的计算机模拟研究
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Sequence similarity between the erythrocyte binding domain of the Plasmodium vivax Duffy binding protein and the V3 loop of HIV-1 strain MN reveals a functional heparin binding motif involved in binding to the Duffy antigen receptor for chemokines.恶性疟原虫红细胞结合蛋白的 Duffy 结合域与 HIV-1 MN 株 V3 环之间的序列相似性揭示了一个功能肝素结合基序,该基序参与与趋化因子的 Duffy 抗原受体结合。
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The promiscuous chemokine binding profile of the Duffy antigen/receptor for chemokines is primarily localized to sequences in the amino-terminal domain.趋化因子的达菲抗原/趋化因子受体杂乱的趋化因子结合谱主要定位于氨基末端结构域的序列。
J Biol Chem. 1995 Nov 3;270(44):26239-45. doi: 10.1074/jbc.270.44.26239.
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The Duffy antigen/receptor for chemokines (DARC) is expressed in endothelial cells of Duffy negative individuals who lack the erythrocyte receptor.趋化因子的达菲抗原/受体(DARC)在缺乏红细胞受体的达菲阴性个体的内皮细胞中表达。
J Exp Med. 1995 Apr 1;181(4):1311-7. doi: 10.1084/jem.181.4.1311.
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Targeting the Plasmodium vivax Duffy-binding protein.靶向间日疟原虫达菲结合蛋白。
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[Molecular basis and structure-activity relationships of the Duffy blood group antigens: chemokine and Plasmodium vivax receptors].[达菲血型抗原的分子基础及构效关系:趋化因子与间日疟原虫受体]
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Sequence similarity between the erythrocyte binding domain 1 of the Plasmodium vivax Duffy binding protein and the V3 loop of HIV-1 strain MN reveals binding residues for the Duffy Antigen Receptor for Chemokines.恶性疟原虫红细胞结合蛋白 1 型 Duffy 结合域与 HIV-1 MN 株 V3 环的序列相似性揭示了趋化因子的 Duffy 抗原受体的结合残基。
Virol J. 2011 Jan 31;8:45. doi: 10.1186/1743-422X-8-45.
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Sulphated tyrosines mediate association of chemokines and Plasmodium vivax Duffy binding protein with the Duffy antigen/receptor for chemokines (DARC).硫酸化酪氨酸介导趋化因子和间日疟原虫达菲结合蛋白与趋化因子达菲抗原/受体(DARC)的结合。
Mol Microbiol. 2005 Mar;55(5):1413-22. doi: 10.1111/j.1365-2958.2004.04478.x.

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