Unexpected modes of PDZ domain scaffolding revealed by structure of nNOS-syntrophin complex
Unexpected modes of PDZ domain scaffolding revealed by structure of nNOS-syntrophin complex
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DOI：
10.1126/science.284.5415.812
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发表时间：
1999-04-30
期刊：
影响因子：
56.9
通讯作者：
Lim, WA
中科院分区：
文献类型：
--
作者：
Hillier, BJ;Christopherson, KS;Lim, WA
神经元型一氧化氮合酶(NNOS)的PDZ蛋白相互作用域与突触后密度蛋白95的PDZ结构域和突触后合营养素的PDZ结构域可以通过不受典型的羧基末端基序识别的相互作用而异源二聚。nNOS-Syntroin PDZ复合体结构揭示了这两个结构域之间以一种不寻常的头到尾的线性排列方式相互作用，nNOS PDZ结构域有两个相反的相互作用面-一个面有典型的多肽结合槽，而另一个面有一个β-发夹“手指”。这个nNOSβ手指停靠在合成素多肽结合槽中，模拟多肽配体，除了急剧的β转弯取代通常需要的羧基末端外，这种结构解释了PDZ结构域如何参与不同的相互作用模式来组装蛋白质网络。
The PDZ protein interaction domain of neuronal nitric oxide synthase (nNOS) can heterodimerize with the PDZ domains of postsynaptic density protein 95 and syntrophin through interactions that are not mediated by recognition of a typical carboxyl-terminal motif, The nNOS-syntrophin PDZ complex structure revealed that the domains interact in an unusual Linear head-to-tail arrangement, The nNOS PDZ domain has two opposite interaction surfaces-one face has the canonical peptide binding groove, whereas the other has a beta-hairpin "finger." This nNOS beta finger docks in the syntrophin peptide binding groove, mimicking a peptide Ligand, except that a sharp beta turn replaces the normally required carboxyl terminus, This structure explains how PDZ domains can participate in diverse interaction modes to assemble protein networks.