GtoPdb v.2023.1趋化因子受体

F. Bachelerie, A. Ben-Baruch, A. Burkhardt, I. Charo, C. Combadière, R. Förster, J. Farber, G. Graham, R. Hills, R. Horuk, M. Locati, A. Luster, A. Mantovani, K. Matsushima, A. Monaghan, G. Moschovakis, P. Murphy, R. Nibbs, H. Nomiyama, Joost J. Oppenheim, C. Power, Amanda E. I. Proudfoot , M. Rosenkilde, A. Rot, S. Sozzani, A. H. Sparre-Ulrich, M. Thelen, Mohib Uddin, O. Yoshie, A. Zlotnik
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引用次数: 0

摘要

趋化因子受体(由NC-IUPHAR趋化因子受体小组委员会商定的命名法[438,437,32])包括一个大的7TM蛋白亚家族,它们结合一种或多种趋化因子,一个大家族的小细胞因子通常对白细胞具有趋化活性。许多趋化因子在胚胎发育、免疫细胞增殖、活化和死亡、病毒感染以及作为抗菌剂等领域的其他造血和非造血作用已被确定。根据功能,趋化因子受体可分为两大类:介导白细胞运输的G蛋白偶联趋化因子受体和“非典型趋化因子受体”,它们可能通过非G蛋白偶联机制发出信号,并作为趋化因子清除剂,下调炎症或形成趋化因子梯度[32]。根据保守半胱氨酸的数量和排列顺序,趋化因子依次可分为四个亚类。CC(也称为β-趋化因子;n= 28), CXC(也称为α-趋化因子;n= 17)和CX3C (n= 1)趋化因子均含有4个保守半胱氨酸,前两个半胱氨酸分别由0、1和3个氨基酸分隔。C趋化因子(n= 2)只含有其他趋化因子中发现的第二和第四半胱氨酸。根据功能,趋化因子也可分为稳态亚群和炎症亚群。大多数趋化因子受体能够结合多个高亲和力的趋化因子配体,但给定受体的配体几乎总是局限于相同的结构亚类。大多数趋化因子与一种以上的受体亚型结合。炎性趋化因子的受体在配体特异性方面通常是高度混杂的,并且可能缺乏选择性的内源性配体。G蛋白偶联趋化因子受体是根据结合的趋化因子类别来命名的,而ACKR是非典型趋化因子受体的词根缩写[33]。在趋化因子和趋化因子受体的序列以及趋化因子受体的药理学和生物学方面,可能存在实质性的跨物种差异。内源性和微生物非趋化因子配体也被鉴定为趋化因子受体。许多趋化因子受体作为HIV共受体发挥作用,但CCR5是唯一一个在HIV/AIDS发病机制中发挥重要作用的趋化因子受体。表格包括标准趋化因子受体名称[693]和别名。
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Chemokine receptors in GtoPdb v.2023.1
Chemokine receptors (nomenclature as agreed by the NC-IUPHAR Subcommittee on Chemokine Receptors [438, 437, 32]) comprise a large subfamily of 7TM proteins that bind one or more chemokines, a large family of small cytokines typically possessing chemotactic activity for leukocytes. Additional hematopoietic and non-hematopoietic roles have been identified for many chemokines in the areas of embryonic development, immune cell proliferation, activation and death, viral infection, and as antibacterials, among others. Chemokine receptors can be divided by function into two main groups: G protein-coupled chemokine receptors, which mediate leukocyte trafficking, and "Atypical chemokine receptors", which may signal through non-G protein-coupled mechanisms and act as chemokine scavengers to downregulate inflammation or shape chemokine gradients [32].Chemokines in turn can be divided by structure into four subclasses by the number and arrangement of conserved cysteines. CC (also known as β-chemokines; n= 28), CXC (also known as α-chemokines; n= 17) and CX3C (n= 1) chemokines all have four conserved cysteines, with zero, one and three amino acids separating the first two cysteines respectively. C chemokines (n= 2) have only the second and fourth cysteines found in other chemokines. Chemokines can also be classified by function into homeostatic and inflammatory subgroups. Most chemokine receptors are able to bind multiple high-affinity chemokine ligands, but the ligands for a given receptor are almost always restricted to the same structural subclass. Most chemokines bind to more than one receptor subtype. Receptors for inflammatory chemokines are typically highly promiscuous with regard to ligand specificity, and may lack a selective endogenous ligand. G protein-coupled chemokine receptors are named acccording to the class of chemokines bound, whereas ACKR is the root acronym for atypical chemokine receptors [33]. There can be substantial cross-species differences in the sequences of both chemokines and chemokine receptors, and in the pharmacology and biology of chemokine receptors. Endogenous and microbial non-chemokine ligands have also been identified for chemokine receptors. Many chemokine receptors function as HIV co-receptors, but CCR5 is the only one demonstrated to play an essential role in HIV/AIDS pathogenesis. The tables include both standard chemokine receptor names [693] and aliases.
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