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1nys
From Proteopedia
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[[Image:1nys.gif|left|200px]] | [[Image:1nys.gif|left|200px]] | ||
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'''Crystal Structure of Activin A Bound to the ECD of ActRIIB P41''' | '''Crystal Structure of Activin A Bound to the ECD of ActRIIB P41''' | ||
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[[Category: Thompson, T B.]] | [[Category: Thompson, T B.]] | ||
[[Category: Woodruff, T K.]] | [[Category: Woodruff, T K.]] | ||
| - | [[Category: | + | [[Category: Activin]] |
| - | [[Category: | + | [[Category: Actriib]] |
| - | [[Category: | + | [[Category: Extracellular domain]] |
| - | [[Category: | + | [[Category: Tgf beta]] |
| - | [[Category: | + | [[Category: Type ii]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 03:09:03 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 00:09, 3 May 2008
Crystal Structure of Activin A Bound to the ECD of ActRIIB P41
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
1NYS 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 Sat May 3 03:09:03 2008
