X-ray structure of TEAD4(E263A+Y429F mutant) complexed with YAP(wildtype): The role of residual flexibility and water molecules in the adaptation of a bound intrinsically disordered protein to mutations at a binding interface
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X-ray structure of TEAD4(E263A+Y429F mutant) complexed with YAP(wildtype): The role of residual flexibility and water molecules in the adaptation of a bound intrinsically disordered protein to mutations at a binding interface Descriptor: MYRISTIC ACID, PHOSPHATE ION, Transcriptional coactivator YAP1, ... Authors: Kallen, J. Deposit date: 2018-04-25 Release date: 2018-09-19 Last modified: 2024-11-20 Method: X-RAY DIFFRACTION (1.8 Å) Cite: Adaptation of the bound intrinsically disordered protein YAP to mutations at the YAP:TEAD interface. Protein Sci., 27, 2018
TEAD4(E263A+Y429F突变体)与野生型YAP复合物的X射线晶体结构：残基柔性与水分子在结合态固有无序蛋白适配结合界面突变过程中的作用。描述项：肉豆蔻酸（MYRISTIC ACID）、磷酸根离子（PHOSPHATE ION）、转录共激活因子YAP1（Transcriptional coactivator YAP1）……作者：Kallen, J.。提交日期：2018-04-25；发布日期：2018-09-19；最后修改日期：2024-11-20。实验方法：X射线衍射（1.8 Å）。引用文献：结合态固有无序蛋白YAP在YAP:TEAD结合界面的突变适配。《Protein Sci.》，27卷，2018年
创建时间：
2018-04-25
