1BTE

CRYSTAL STRUCTURE OF THE EXTRACELLULAR DOMAIN OF THE TYPE II ACTIVIN RECEPTOR

Summary for 1BTE

• Entry DOI: 10.2210/pdb1bte/pdb
• Descriptor: PROTEIN (ACTIVIN RECEPTOR TYPE II), 2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total)
• Functional Keywords: receptor, serine kinase, ligand binding domain, three-finger toxin, transferase
• Biological source: Mus musculus (house mouse)
• Total number of polymer chains: 2
• Total formula weight: 23900.44

Authors

Greenwald, J.,Fischer, W.,Vale, W.,Choe, S. (deposition date: 1998-09-01, release date: 1999-02-09, Last modification date: 2024-10-30)

Primary citation

Greenwald, J.,Fischer, W.H.,Vale, W.W.,Choe, S.
Three-finger toxin fold for the extracellular ligand-binding domain of the type II activin receptor serine kinase.
Nat.Struct.Biol., 6:18-22, 1999

PubMed Abstract: 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.

PubMed: 9886286
DOI: 10.1038/4887

Experimental method

X-RAY DIFFRACTION (1.5 Å)