Peptide-in-groove interactions link target proteins to the β-propeller of clathrin
Peptide-in-groove interactions link target proteins to the β-propeller of clathrin
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DOI：
10.1073/pnas.97.3.1096
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发表时间：
2000-02-01
影响因子：
11.1
通讯作者：
Kirchhausen, T
中科院分区：
文献类型：
--
作者：
ter Haar, E;Harrison, SC;Kirchhausen, T
“WD40”结构域是一种广泛的识别模块，用于连接细胞内信号和分类网络中的伙伴蛋白。笼状蛋白氨基末端结构域指导货物进入涂层坑，是一种在结构上与WD40模块密切相关的贝塔推进器。结晶学测定的网状蛋白末端结构域与来自两个不同货物适配器的多肽-β-arrestin 2和AP-3复合体的β-亚基的结构显示出惊人的相似的多肽-沟槽相互作用。我们结构中的两个多肽包含相关的五个残基基序，这些基序构成了它们与笼状蛋白接触的核心。许多其他参与内吞作用的蛋白质都有类似的“网状蛋白-盒”基序，因此它们很可能都以相同的方式结合到末端区域。我们认为，槽中肽相互作用是β推进器识别特定靶蛋白的一种重要的一般模式。
The "WD40" domain is a widespread recognition module for linking partner proteins in intracellular networks of signaling and sorting. The clathrin amino-terminal domain, which directs incorporation of cargo into coated pits, is a beta-propeller closely related in structure to WD40 modules. The crystallographically determined structures of complexes of the clathrin-terminal domain with peptides derived from two different cargo adaptors, beta-arrestin 2 and the beta-subunit of the AP-3 complex, reveal strikingly similar peptide-in-groove interactions. The two peptides in our structures contain related, five-residue motifs, which form the core of their contact with clathrin. A number of other proteins involved in endocytosis have similar "clathrin-box" motifs, and it therefore is likely that they all bind the terminal domain in the same way. We propose that a peptide-in-groove interaction is an important general mode by which beta-propellers recognize specific target proteins.