The repeat region of cortactin is intrinsically disordered in solution.
The repeat region of cortactin is intrinsically disordered in solution.
复制标题
Cortactin 的重复区域在溶液中本质上是无序的。
DOI：
10.1038/s41598-017-16959-1
复制
发表时间：
2017
影响因子：
4.6
通讯作者：
Boggon,TitusJ
中科院分区：
文献类型：
--
作者：
Li,Xiaofeng;Tao,Yeqing;Murphy,JamesW;Scherer,AlexanderN;Lam,TuKietT;Marshall,AlanG;Koleske,AnthonyJ;Boggon,TitusJ
The multi-domain protein, cortactin, contains a 37-residue repeating motif that binds to actin filaments. This cortactin repeat region comprises 6½ similar copies of the motif and binds actin filaments. To better understand this region of cortactin, and its fold, we conducted extensive biophysical analysis. Size exclusion chromatography with multi-angle light scattering (SEC-MALS) reveals that neither constructs of the cortactin repeats alone or together with the adjacent helical region homo-oligomerize. Using circular dichroism (CD) we find that in solution the cortactin repeats resemble a coil-like intrinsically disordered protein. Small-angle X-ray scattering (SAXS) also indicates that the cortactin repeats are intrinsically unfolded, and the experimentally observed radius of gyration (Rg) is coincidental to that calculated by the program Flexible-Meccano for an unfolded peptide of this length. Finally, hydrogen-deuterium exchange mass spectrometry (HDX-MS) indicates that the domain contains limited hydrophobic core regions. These experiments therefore provide evidence that in solution the cortactin repeat region of cortactin is intrinsically disordered.
