STIL蛋白包含介导其蛋白质-蛋白质相互作用的内在无序区域。
The STIL protein contains intrinsically disordered regions that mediate its protein-protein interactions.
作者信息
Amartely Hadar, David Ahuvit, Lebendiker Mario, Benyamini Hadar, Izraeli Shai, Friedler Assaf
机构信息
Institute of Chemistry, The Hebrew University of Jerusalem, Safra Campus, Givat Ram, Jerusalem 91904, Israel.
出版信息
Chem Commun (Camb). 2014 May 25;50(40):5245-7. doi: 10.1039/c3cc45096a. Epub 2013 Sep 11.
The STIL protein participates in mitosis and malignant transformation by regulating centrosomal duplication. Using biophysical methods we studied the structure and interactions of STIL. We revealed that its central domain is intrinsically disordered and mediates protein-protein interactions of STIL. The intrinsic disorder may provide STIL with the conformational flexibility required for its multitude binding.
STIL蛋白通过调节中心体复制参与有丝分裂和恶性转化。我们使用生物物理方法研究了STIL的结构和相互作用。我们发现其中心结构域是内在无序的，并介导STIL的蛋白质-蛋白质相互作用。这种内在无序可能为STIL提供其多种结合所需的构象灵活性。
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