1bte | pdb_00001bte
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
Page seeded by OCA on Tue Nov 20 11:54:27 2007
