A motif in LILRB2 critical for Angptl2 binding and activation

Author:

Deng Mi1,Lu Zhigang12,Zheng Junke13,Wan Xuan1,Chen Xiaoli1,Hirayasu Kouyuki4,Sun Hanzi5,Lam Yeeling1,Chen Liping1,Wang Qihui6,Song Chun7,Huang Niu5,Gao George F.6,Jiang Youxing1,Arase Hisashi4,Zhang Cheng Cheng18

Affiliation:

1. Department of Physiology, University of Texas Southwestern Medical Center, Dallas, TX;

2. Laboratory of Chemical Genomics, School of Chemical Biology and Biotechnology, Shenzhen Graduate School of Peking University, Shenzhen, China;

3. Department of Pathophysiology, Shanghai Universities E-Institute for Chemical Biology, Key Laboratory of Cell Differentiation and Apoptosis of Chinese Ministry of Education, Shanghai Jiao Tong University School of Medicine, Shanghai, China;

4. Department of Immunochemistry, Research Institute for Microbial Diseases and Laboratory of Immunochemistry, World Premier International Immunology Frontier Research Center, Osaka University, and Core Research for Evolutional Science and Technology, Japan Science and Technology Agency, Osaka, Japan;

5. National Institute of Biological Sciences, Beijing, China;

6. Chinese Academy of Sciences Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing, China;

7. Shandong University and National New Drug R&D Center in Shandong, Jinan, China; and

8. Department of Developmental Biology, University of Texas Southwestern Medical Center, Dallas, TX

Abstract

Key Points A motif in the immunoglobulin domains of LILRB2 is critical to the multimerized Angptl2 binding and signaling activation. Immobilized anti-LILRB2 supports ex vivo expansion of human cord blood HSCs.

Publisher

American Society of Hematology

Subject

Cell Biology,Hematology,Immunology,Biochemistry

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