1NYU

Crystal Structure of Activin A Bound to the ECD of ActRIIB

Summary for 1NYU

• Entry DOI: 10.2210/pdb1nyu/pdb
• Related: 1NYS
• Descriptor: activin receptor, Inhibin beta A chain (2 entities in total)
• Functional Keywords: activin, type ii, tgf beta, actriib, extracellular domain, membrane protein-hormone-growth factor complex, membrane protein/hormone/growth factor
• Biological source: Rattus norvegicus (Norway rat); More
• Cellular location: Cell membrane ; Single-pass type I membrane protein : P38445; Secreted: P08476
• Total number of polymer chains: 4
• Total formula weight: 50666.92

Authors

Thompson, T.B.,Woodruff, T.K.,Jardetzky, T.S. (deposition date: 2003-02-13, release date: 2003-04-08, Last modification date: 2023-08-16)

Primary citation

Thompson, T.B.,Woodruff, T.K.,Jardetzky, T.S.
Structures of an ActRIIB:activin A complex reveal a novel binding mode for TGF-beta ligand:receptor interactions
EMBO J., 22:1555-1566, 2003

PubMed Abstract: The TGF-beta superfamily of ligands and receptors stimulate cellular events in diverse processes ranging from cell fate specification in development to immune suppression. Activins define a major subgroup of TGF-beta ligands that regulate cellular differentiation, proliferation, activation and apoptosis. Activins signal through complexes formed with type I and type II serine/threonine kinase receptors. We have solved the crystal structure of activin A bound to the extracellular domain of a type II receptor, ActRIIB, revealing the details of this interaction. ActRIIB binds to the outer edges of the activin finger regions, with the two receptors juxtaposed in close proximity, in a mode that differs from TGF-beta3 binding to type II receptors. The dimeric activin A structure differs from other known TGF-beta ligand structures, adopting a compact folded-back conformation. The crystal structure of the complex is consistent with recruitment of two type I receptors into a close packed arrangement at the cell surface and suggests that diversity in the conformational arrangements of TGF-beta ligand dimers could influence cellular signaling processes.

PubMed: 12660162
DOI: 10.1093/emboj/cdg156

Experimental method

X-RAY DIFFRACTION (3.1 Å)