Thermodynamic analysis of degenerate recognition by the NKG2D immunoreceptor: Not induced fit but rigid adaptation
Thermodynamic analysis of degenerate recognition by the NKG2D immunoreceptor: Not induced fit but rigid adaptation
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DOI：
10.1016/s1074-7613(03)00320-0
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发表时间：
2003-12-01
期刊：
影响因子：
32.4
通讯作者：
Strong, RK
中科院分区：
文献类型：
--
作者：
McFarland, BJ;Strong, RK
同型二聚体免疫受体NKG 2D在与多种条件表达的MHC I类样蛋白配体接合后驱动效应细胞的活化。NKG 2D识别是高度简并的，因为受体单体上的单个表面结合每个结构不同配体上的不同表面对，同时容纳多个非保守配体等位基因或同种型取代。与TCR-pMHC和其他NK受体-配体相互作用相反，本文报告的四种NKG 2D-配体对（MIC-A*001、MIC-B*005、ULBP 1和RAE-1 β）的热力学和动力学分析表明，相对热力学和熵项、热容、结合速率和活化能势垒与典型的刚性蛋白质-蛋白质相互作用相当。NKG 2D简并性不是“诱导拟合”结合，而是在每个刚性界面处使用不同的相互作用机制实现的。
The homodimeric immunoreceptor NKG2D drives the activation of effector cells following engagement of diverse, conditionally expressed MHC class I-like protein ligands. NKG2D recognition is highly degenerate in that a single surface on receptor monomers binds pairs of distinct surfaces on each structurally divergent ligand, simultaneously accommodating multiple nonconservative ligand allelic or isoform substitutions. In contrast to TCR-pMHC and other NK receptor-ligand interactions, thermodynamic and kinetic analyses of four NKG2D-ligand pairs (MIC-A*001, MIC-B*005, ULBP1, and RAE-1beta) reported here show that the relative enthalpic and entropic terms, heat capacity, association rates, and activation energy barriers are comparable to typical, rigid protein-protein interactions. Rather than "induced-fit" binding, NKG2D degeneracy is achieved using distinct interaction mechanisms at each rigid interface.