Self-recognition by an intrinsically disordered protein.
Self-recognition by an intrinsically disordered protein.
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通过本质上无序的蛋白质进行自我识别。
DOI：
10.1016/j.febslet.2008.06.022
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发表时间：
2008
期刊：
影响因子：
3.5
通讯作者：
Hecht O
中科院分区：
文献类型：
--
作者：
Hecht O
蛋白质抗生素大肠杆菌素N的固有无序易位结构域（T-结构域）结合至靶大肠杆菌细胞的周质受体以穿透它们的内膜。我们在这里报告，大肠杆菌素N的T-结构域的特定27个连续残基已知结合到靶细胞中的辅助蛋白托拉也与大肠杆菌素N的折叠区域分子内相互作用。我们认为，这种特定的自我识别有助于内在无序的结构域埋葬他们的疏水识别基序，并保护他们免受降解，表明受损的自我识别导致蛋白酶敏感性增加。
The intrinsically disordered translocation domain (T-domain) of the protein antibiotic colicin N binds to periplasmic receptors of target Escherichia coli cells in order to penetrate their inner membranes. We report here that the specific 27 consecutive residues of the T-domain of colicin N known to bind to the helper protein TolA in target cells also interacts intramolecularly with folded regions of colicin N. We suggest that this specific self-recognition helps intrinsically disordered domains to bury their hydrophobic recognition motifs and protect them against degradation, showing that an impaired self-recognition leads to increased protease susceptibility.