PROLYL ISOMERASE PIN1S INTERACTION W/ MITOTICALLY PHOSPHORYLATED SUBSTRATES

结合1.35 E晶体结构的功能研究 Pin 1显示对磷酸化的Ser/Thr的优先选择， 在其靶向选择中N-末端至脯氨酸。 努力 可视化这些相互作用，并阐明Pin 1的机制 介导的肽键异构化， Pin 1-肽复合物以及Pin 1晶体与 磷酸-丝氨酸-脯氨酸二肽。 泛素连接酶（E3）决定了 泛素介导的蛋白质降解的选择性。 结构 对这些泛素连接酶的研究对于阐明它们的 反应机制，最重要的是它们的目标模式 选择. 我们已经生长了Nedd 4样泛素连接酶的晶体， Hect-domain，空间群P1。

Functional studies combined with the 1.35 E crystal structure of Pin1 show a preference for a phosphorylated Ser/Thr immediately N-terminal to proline in its target selection. In efforts to visualize these interactions and clarify the mechanism of Pin1 mediated peptide bond isomerization we have begun co-crystallization of Pin1-peptide complexes as well as soaks of Pin1 crystals with phospho-Ser-Pro dipeptides. Ubiquitin ligases (E3) determine the selectivity of ubiquitin-mediated protein degradation. Structural studies of these ubiquitin ligases are crucial in elucidating their reaction mechanisms and most importantly their mode of target selection. We have grown crystals of the Nedd4-like ubiquitin ligase hect-domain in space group P1.