The interleukin 2 receptor. Functional consequences of its bimolecular structure.

The interleukin 2 receptor. Functional consequences of its bimolecular structure.
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DOI:
10.1084/jem.166.4.1055
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发表时间:
1987-10-01
影响因子:
15.3
通讯作者:
SMITH, KA
SMITH, KA
中科院分区:
医学1区
文献类型:
--
作者:
WANG, HM;SMITH, KA

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高亲和力的IL-2-R结合源于两种称为α和β的il -2结合蛋白之间的特殊类型的合作相互作用。当在细胞表面一起表达时,这两条不同的链形成一个非共价的动态杂交受体复合物,利用p55 β链的快速结合率和p75 α链的缓慢解离率特征。p75 α链是细胞生长的信号,而p55 β链仅作为辅助结合位点促进IL-2的结合,本身没有明显的信号作用。这种结构组织的独特功能暗示表明,这种合作的双分子排列反映了一种普遍的机制,通过这种机制,表面受体的效率可以显著提高。
High-affinity IL-2-R binding results from an exceptional type of cooperative interaction between two IL-2-binding proteins termed alpha and beta. When expressed together on the cell surface, these two distinct chains form a noncovalent kinetic hybrid receptor complex that exploits a rapid association rate contributed by the p55 beta chain and a slow dissociation rate characteristic for the p75 alpha chain. The p75 alpha chains signal cell growth, whereas the p55 beta chains only facilitate IL-2 binding by serving as helper binding sites, having no discernible signaling role themselves. The unique functional implications of this structural organization indicate that this cooperative bimolecular arrangement reflects a general mechanism by which the efficiency of surface receptors can be enhanced markedly.
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发表时间: 1984-10-01
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