Structure and function of immunoglobulins.
Structure and function of immunoglobulins.
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DOI：
10.1016/j.jaci.2009.09.046
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发表时间：
2010-02
影响因子：
14.2
通讯作者：
Cavacini, Lisa
中科院分区：
文献类型：
--
作者：
Schroeder, Harry W., Jr.;Cavacini, Lisa
关键词：
免疫球蛋白是由两条重链（H）和两条轻链（L）组成的异二聚体蛋白。它们可以在功能上分为结合抗原的可变（V）结构域和指定效应子功能（例如补体激活或结合Fc受体）的恒定（C）结构域。可变结构域通过一系列复杂的基因重排事件产生，然后可以在暴露于抗原后进行体细胞超突变以允许亲和力成熟。每个V结构域可以分成三个序列可变性区域，称为互补决定区或CDR，和四个相对恒定序列区域，称为框架区或FR。H链的三个CDR与L链的三个CDR配对以形成抗原结合位点，如经典定义。重链C结构域主要有五类。每个类别定义IgM、IgG、伊加、IgD和IgE同种型。IgG可以分为四个亚类，IgG 1，IgG 2，IgG 3和IgG 4，每个亚类都有自己的生物学特性;伊加可以类似地分为IgA 1和IgA 2。H链的恒定结构域可以被转换以允许改变效应子功能，同时保持抗原特异性。
Immunoglobulins are heterodimeric proteins composed of two heavy (H) and two light (L) chains. They can be separated functionally into variable (V) domains that binds antigens and constant (C) domains that specify effector functions such as activation of complement or binding to Fc receptors. The variable domains are created by means of a complex series of gene rearrangement events, and can then be subjected to somatic hypermutation after exposure to antigen to allow affinity maturation. Each V domain can be split into three regions of sequence variability, termed the complementarity determining regions, or CDRs, and four regions of relatively constant sequence termed the framework regions, or FRs. The three CDRs of the H chain are paired with the three CDRs of the L chain to form the antigen binding site, as classically defined. There are five main classes of heavy chain C domains. Each class defines the IgM, IgG, IgA, IgD, and IgE isotypes. IgG can be split into four subclasses, IgG1, IgG2, IgG3, and IgG4, each with its own biologic properties; and IgA can similarly be split into IgA1 and IgA2. The constant domains of the H chain can be switched to allow altered effector function while maintaining antigen specificity.
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影响因子：
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DOI：
10.1073/pnas.0810163105
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