1nyu
From Proteopedia
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Crystal Structure of Activin A Bound to the ECD of ActRIIB
Overview
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.
About this Structure
1NYU is a Protein complex structure of sequences from Homo sapiens and Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
Structures of an ActRIIB:activin A complex reveal a novel binding mode for TGF-beta ligand:receptor interactions., Thompson TB, Woodruff TK, Jardetzky TS, EMBO J. 2003 Apr 1;22(7):1555-66. PMID:12660162
Page seeded by OCA on Mon Nov 12 18:27:08 2007
