1nyu
From Proteopedia
(New page: 200px<br /> <applet load="1nyu" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nyu, resolution 3.10Å" /> '''Crystal Structure o...) |
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| - | [[Image:1nyu.gif|left|200px]]<br /> | + | [[Image:1nyu.gif|left|200px]]<br /><applet load="1nyu" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1nyu" size=" | + | |
caption="1nyu, resolution 3.10Å" /> | caption="1nyu, resolution 3.10Å" /> | ||
'''Crystal Structure of Activin A Bound to the ECD of ActRIIB'''<br /> | '''Crystal Structure of Activin A Bound to the ECD of ActRIIB'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The TGF-beta superfamily of ligands and receptors stimulate cellular | + | 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== | ==About this Structure== | ||
| - | 1NYU is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http:// | + | 1NYU is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NYU OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
| - | [[Category: Jardetzky, T | + | [[Category: Jardetzky, T S.]] |
| - | [[Category: Thompson, T | + | [[Category: Thompson, T B.]] |
| - | [[Category: Woodruff, T | + | [[Category: Woodruff, T K.]] |
[[Category: activin]] | [[Category: activin]] | ||
[[Category: actriib]] | [[Category: actriib]] | ||
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[[Category: type ii]] | [[Category: type ii]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:11:34 2008'' |
Revision as of 12:11, 21 February 2008
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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 Thu Feb 21 14:11:34 2008
