施一公973项目最新《Nature》子刊文章

　　

生物通报道，据悉，海外杰出学者施一公回国后在清华大学建立了自己的实验室，近期，他在新的实验室以清华的名义发表的文章刊登在Nature子刊，Nature Structure & Molecular biology2008年12月14日online版上，文章题为：Crystal structure of TIPE2 provides insight into Immune homeostasis。

 

TNFAIP8-like 2（TIPE2）在维持免疫内环境的过程具有重要的意义，但是关于TIPE2的工作机制至今不明晰。

 

施一公的研究小组对TIPE2的晶体结构进行了分析，发现其真实的蛋白折叠结构与先前用软件预测的折叠结构有出入，尤其是该蛋白的死亡效应区域（death effector domain）结构。明显的，TIPE2蛋白具有一个巨大的疏水中央腔体结构，该区域具有协助蛋白结合的功能。探明TIPE2蛋白的结构的意义在于深入了解TIPE2蛋白的功能和作用机制，并且对TNFAIP8蛋白家族的结构预测也具有借鉴指导意义。

 

生物通  张欢

 

原文检索：Crystal structure of TIPE2 provides insights into immune homeostasis

Xu Zhang1, Jiawei Wang1, Chao Fan1, Hubo Li1, Honghong Sun2, Shunyou Gong2, Youhai H Chen2 & Yigong Shi1,3

 

【Abstract】

TNFAIP8-like 2 (TIPE2) has an essential role in immune homeostasis, yet the underlying mechanism remains enigmatic. The high-resolution crystal structure of TIPE2 reveals a previously uncharacterized fold that is different from the predicted fold of a death effector domain (DED). Strikingly, TIPE2 contains a large, hydrophobic central cavity that is poised for cofactor binding. These structural features will be important for understanding the functions of TIPE2 and other TNFAIP8 family proteins.

 

1Center for Structural Biology and Department of Biological Sciences and Biotechnology, Tsinghua University, Beijing 100084, China.

2Department of Pathology and Laboratory Medicine, University of Pennsylvania, Philadelphia, Pennsylvania 19104, USA. 3Tsinghua University School of Medicine, Beijing 100084, China.

Correspondence should be addressed to Y.S. ([e-mail]).