Zinc Links in a Receptor-Kinase Complex

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Abstract

Association of the T cell coreceptors CD-4 and CD-8 with the cytoplasmic kinase Lck regulates T cell activation and maturation. Kim et al. have explored the requirement for zinc in this interaction and report that the metal ion acts as a clasp that stabilizes a receptor-Lck complex. Peptides corresponding to a short region of Lck and in either receptor's cytoplasmic tail were unordered, but the presence of zinc induced the synergistic mutual folding of the peptides. Protein modifications could unlatch the clasp and modulate receptor-Lck binding. P. W. Kim, Z.-Y. J. Sun, S. C. Blacklow, G. Wagner, M. J. Eck, A zinc clasp structure tethers Lck to T cell coreceptors CD4 and CD8. Science 301, 1725-1728 (2003). [Abstract] [Full Text]
受体激酶复合物中的锌连接
T细胞共受体CD-4和CD-8与细胞质激酶Lck的关联调节T细胞的激活和成熟。Kim等人研究了这种相互作用中对锌的需求,并报道了金属离子作为稳定受体- lck复合物的扣环。与Lck短区域和受体细胞质尾部对应的肽是无序的,但锌的存在诱导了肽的协同相互折叠。蛋白质修饰可以解开锁扣并调节受体- lck结合。金宝文,张志勇。孙建军,孙建军,李建军,等。T细胞辅助受体CD4和CD8的锌扣结构研究。科学31,1725-1728(2003)。【摘要】【全文】
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