Schulman Brenda A, Chen Zhijian J
Howard Hughes Medical Institute, St. Jude Children's Research Hospital, 332 North Lauderdale Street, Memphis, Tennessee 38105, USA.
Mol Cell. 2005 Dec 9;20(5):653-5. doi: 10.1016/j.molcel.2005.11.019.
CHIP is a ubiquitin ligase implicated in the degradation of misfolded proteins. In the November 23 issue of Molecular Cell, identified CHIP as a protein that interacts with the ubiquitin E2 complex Ubc13-Uev1A, which catalyzes the synthesis of Lys-63-linked polyubiquitin chains. Although the ubiquitin ligase activity of CHIP requires its dimerization through the U box domain, the crystal structure of the CHIP-E2 complex reveals that the protomers in the CHIP homodimer adopt distinct conformations such that only one U box of CHIP interacts with Ubc13.
CHIP是一种参与错误折叠蛋白降解的泛素连接酶。在11月23日的《分子细胞》杂志上，研究人员将CHIP鉴定为一种与泛素E2复合物Ubc13-Uev1A相互作用的蛋白质，该复合物催化赖氨酸63连接的多聚泛素链的合成。尽管CHIP的泛素连接酶活性需要其通过U盒结构域二聚化，但CHIP-E2复合物的晶体结构显示，CHIP同型二聚体中的原体采用不同的构象，使得CHIP只有一个U盒与Ubc13相互作用。
