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Crystal structure of TIPE2 provides insights into immune homeostasis

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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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Figure 1: The structure of TIPE2 defines a previously uncharacterized fold that is different from the DED.
Figure 2: TIPE2 contains a centrally located, hydrophobic cavity that may have an important role in immune homeostasis.

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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.).

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Authors and Affiliations

Authors

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.

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Correspondence to Yigong Shi.

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Supplementary Figures 1–3, Supplementary Table 1 and Supplementary Methods (PDF 446 kb)

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Zhang, X., Wang, J., Fan, C. et al. Crystal structure of TIPE2 provides insights into immune homeostasis. Nat Struct Mol Biol 16, 89–90 (2009). https://doi.org/10.1038/nsmb.1522

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