The mode of Hedgehog binding to Ihog homologues is not conserved across different phyla

Jason S. McLellan, Xiaoyan Zheng, Glenn Hauk, Rodolfo Ghirlando, Philip A. Beachy and Daniel J. Leahy ()
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Jason S. McLellan: Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA
Xiaoyan Zheng: and
Glenn Hauk: Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA
Rodolfo Ghirlando: Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Disease, National Institutes of Health, Bethesda, Maryland 20892, USA
Philip A. Beachy: and
Daniel J. Leahy: Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA

Nature, 2008, vol. 455, issue 7215, 979-983

Abstract: Hedgehog signalling: variations on the theme The Hedgehog signalling pathway specifies tissue pattern in metazoan embryos. Intriguingly, the crystal structure of the human Sonic Hedgehog protein Shh complexed with a fragment of the cell surface protein CDO (the vertebrate equivalent of Ihog in Drosophila) reveals that the mode of Hedgehog binding to Ihog homologues is not conserved across different phyla. The interaction between human Shh and CDO involves a previously unrecognized calcium-binding site in Shh that is buried at the interface between the two proteins. Mutations in Shh causing congenital malformations map to the calcium-binding site and disrupt interactions with binding partners.

Date: 2008
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DOI: 10.1038/nature07358

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