the structure of tumor endothelial marker 8 (tem8) extracellular domain and implications for its receptor function for recognizing anthrax toxin结构的肿瘤血管内皮标记8(八级)细胞外域和对其识别炭疽毒素受体功能的影响.pdfVIP

The Structure of Tumor Endothelial Marker 8 (TEM8) Extracellular Domain and Implications for Its Receptor Function for Recognizing Anthrax Toxin 1,2. 1,2. 3 2 1,2 1,2 3 Sheng Fu , Xiaohang Tong , Chenguang Cai , Ying Zhao , Yang Wu , Yuanyuan Li , Junjie Xu , 1 4 3 1,2,5 Xuejun C. Zhang , Long Xu , Wei Chen *, Zihe Rao * 1 National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, China, 2 Laboratory of Structural Biology, Tsinghua University, Beijing, China, 3 State Key Laboratory of Pathogen and Biosecurity, Beijing Institute of Microbiology and Epidemiology, Beijing, China, 4 Laboratory of Protein Engineering, Beijing Institute of Biotechnology, Beijing, China, 5 College of Sciences and Tianjin State Laboratory of Protein Sciences, Nankai University, Tianjin, China Abstract Anthrax toxin, which is released from the Gram-positive bacterium Bacillus anthracis, is composed of three proteins: protective antigen (PA), lethal factor (LF), and edema factor (EF). PA binds a receptor on the surface of the target cell and further assembles into a homo-heptameric pore through which EF and LF translocate into the cytosol. Two distinct cellular receptors for anthrax toxin, TEM8/ANTXR1 and CMG2/ANTXR2, have been identified, and it is known that their extracellular domains bind PA with low and high affinities, respectively. Here, we report the crystal structure of the TEM8 extracellular ˚ vWA domain at 1.7 A resolution. The overall structure has a typical integrin fold and is similar to that of the previou