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Solution structure of the PX domain, a target of the SH3 domain

Nature Structural Biology volume 8, pages 526–530 (2001)Cite this article

Abstract

The phox homology (PX) domain is a novel protein module containing a conserved proline-rich motif. We have shown that the PX domain isolated from the human p47phox protein, a soluble subunit of phagocyte NADPH oxidase, binds specifically to the C-terminal SH3 domain derived from the same protein. The solution structure of p47 PX has an α + β structure with a novel folding motif topology and reveals that the proline-rich motif is presented on the molecular surface for easy recognition by the SH3 domain. The proline-rich motif of p47 PX in the free state adopts a distorted left-handed polyproline type II helix conformation.

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Figure 1: Domain structure of the human p47phox protein and sequence alignment of the PX domains.
Figure 2: In vitro interactions of the p47 PX and the p47 C-terminal SH3.
Figure 3: Structure of the p47 PX domain.
Figure 4: NMR analysis of the interaction of the p47 PX domain and the C-terminal SH3 domain.

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Acknowledgements

We thank H. Nakamura for the program EMBOSS.

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Authors and Affiliations

  1. Department of Structural Biology, Biomolecular Engineering Research Institute, 6-2-3, Furuedai, Suita, Osaka, 565-0874, Japan

    Hidekazu Hiroaki & Daisuke Kohda

  2. Department of Molecular and Structural Biology, Kyushu University Graduate School of Medicinal Science, 3-1-1 Maidashi, Higashi-ku, Fukuoka, 812-0082, Japan

    Tetsuro Ago & Hideki Sumimoto

  3. Cancer Research Institute, Kanazawa University, 13-1, Takaramachi, Kanazawa, 920-0934, Japan

    Takashi Ito

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  1. Hidekazu Hiroaki
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Correspondence to Daisuke Kohda.

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Hiroaki, H., Ago, T., Ito, T. et al. Solution structure of the PX domain, a target of the SH3 domain. Nat Struct Mol Biol 8, 526–530 (2001). https://doi.org/10.1038/88591

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