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Letter
Nature Structural Biology  6, 18 - 22 (1999)
doi:10.1038/4887

Three-finger toxin fold for the extracellular ligand-binding domain of the type II activin receptor serine kinase.

Jason Greenwald1, 3, Wolfgang H. Fischer2, Wylie W. Vale2 & Senyon Choe1, 3

1  Structural Biology Laboratory, The Salk Institute, La Jolla, California 92037, USA.

2  Clayton Foundation Laboratories for Peptide Biology, The Salk Institute, La Jolla, California 92037, USA.

3  Department of Chemistry and Biochemistry, University of California, San Diego, La Jolla, California 92093, USA.

Correspondence should be addressed to Senyon Choe choe@sbl.salk.edu
The transforming growth factor beta (TGFbeta) superfamily of cytokines elicit diverse biological responses by interacting with two distinct, but structurally related transmembrane receptor serine kinases (type I and type II). The binding of these dimeric ligands to the type II receptor is the first event in transmembrane signaling for this family. Here we report the 1.5 Å resolution crystal structure of the extracellular ligand-binding domain of the type II activin receptor (ActRII-ECD), which reveals a fold similar to that of a class of toxins known as three-finger toxins. This fold is primarily dictated by disulfide bonds formed by eight conserved cysteines, with a characteristic spacing, and thus is likely to be shared by most of the type I and II receptors for the TGFbeta family. Sequence comparison with an evolutionarily distant activin binding-protein identifies several conserved residues, including two hydrophobic clusters that may form binding surfaces for activin and the type I receptor.

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Nature Structural & Molecular Biology
ISSN: 1545-9993
EISSN: 1545-9985
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