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Crystal structure of TIPE2 provides insights into immune homeostasis

Nature Structural & Molecular Biology volume 16, pages 8990 (2009) | Download Citation

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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.

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Acknowledgements

We thank N. Shimizu at the Spring-8 beamline BL41XU and T. Kumasaka and S. Baba at beamline BL38XU for help. This work was supported by funds from Tsinghua University (Y.S.).

Author information

Affiliations

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

    • Xu Zhang
    • , Jiawei Wang
    • , Chao Fan
    • , Hubo Li
    •  & Yigong Shi
  2. Department of Pathology and Laboratory Medicine, University of Pennsylvania, Philadelphia, Pennsylvania 19104, USA.

    • Honghong Sun
    • , Shunyou Gong
    •  & Youhai H Chen
  3. Tsinghua University School of Medicine, Beijing 100084, China.

    • Yigong Shi

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Contributions

X.Z. carried out biochemistry experiments, crystallization and data analysis and prepared the manuscript; J.W. carried out structure determination; C.F. and H.L. assisted X.Z.; H.S., S.G. and Y.H.C. were involved in collaboration and discussion; and Y.S. supervised the research and prepared the manuscript.

Corresponding author

Correspondence to Yigong Shi.

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    Supplementary Figures 1–3, Supplementary Table 1 and Supplementary Methods

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DOI

https://doi.org/10.1038/nsmb.1522

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