1bte
From Proteopedia
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CRYSTAL STRUCTURE OF THE EXTRACELLULAR DOMAIN OF THE TYPE II ACTIVIN RECEPTOR
Overview
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 A 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.
About this Structure
1BTE is a Single protein structure of sequence from Mus musculus with NAG as ligand. Full crystallographic information is available from OCA.
Reference
Three-finger toxin fold for the extracellular ligand-binding domain of the type II activin receptor serine kinase., Greenwald J, Fischer WH, Vale WW, Choe S, Nat Struct Biol. 1999 Jan;6(1):18-22. PMID:9886286
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