1nyu: Difference between revisions

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[[Image:1nyu.gif|left|200px]]
{{Seed}}
[[Image:1nyu.png|left|200px]]


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{{STRUCTURE_1nyu|  PDB=1nyu  |  SCENE=  }}  
{{STRUCTURE_1nyu|  PDB=1nyu  |  SCENE=  }}  


'''Crystal Structure of Activin A Bound to the ECD of ActRIIB'''
===Crystal Structure of Activin A Bound to the ECD of ActRIIB===




==Overview==
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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.
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{{ABSTRACT_PUBMED_12660162}}


==About this Structure==
==About this Structure==
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[[Category: Tgf beta]]
[[Category: Tgf beta]]
[[Category: Type ii]]
[[Category: Type ii]]
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