Sakihama T, Smolyar A, Reinherz E L
Laboratory of Immunobiology, Dana-Farber Cancer Institute, Boston, MA, USA.
Immunol Today. 1995 Dec;16(12):581-7. doi: 10.1016/0167-5699(95)80081-6.
Recent evidence indicates that CD4 stably binds to major histocompatibility complex (MHC) class II only after assuming an oligomeric state: the membrane-distal CD4 D1-D2 module interacts directly with MHC class II, whereas the membrane-proximal CD4 D3-D4 module mediates oligomerization. This results in the formation of aggregates critical for T-cell activation. The T-cell receptor (TCR) regulates specific crosslinking and is itself dependent on lattice formation to trigger physiological T-cell responses. Here, Toshiko Sakihama, Alex Smolyar and Ellis Reinherz discuss the molecular nature of CD4-MHC class II clustering and how, despite each of the component interactions being of low affinity, the molecular matrix renders T-cell recognition extremely specific and sensitive.
最近的证据表明，CD4只有在形成寡聚体状态后才会稳定地与主要组织相容性复合体（MHC）II类结合：膜远端的CD4 D1-D2模块直接与MHC II类相互作用，而膜近端的CD4 D3-D4模块介导寡聚化。这导致形成对T细胞活化至关重要的聚集体。T细胞受体（TCR）调节特异性交联，其本身也依赖于晶格形成来触发生理性T细胞反应。在此，坂浜俊子、亚历克斯·斯莫利亚尔和埃利斯·赖因赫兹讨论了CD4-MHC II类聚集的分子本质，以及尽管每个组分间的相互作用亲和力较低，但分子基质如何使T细胞识别极其特异且敏感。
