1nyu: Difference between revisions

Revision as of 15:11, 21 February 2008

Crystal Structure of Activin A Bound to the ECD of ActRIIB

OverviewOverview

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 StructureAbout this Structure

1NYU is a Protein complex structure of sequences from Homo sapiens and Rattus norvegicus. Full crystallographic information is available from OCA.

ReferenceReference

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

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OCA

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 '''Crystal Structure of Activin A Bound to the ECD of ActRIIB'''<br />
 ==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.
+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==
-NYU 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1NYU OCA].
+NYU 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==
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 [[Category: Protein complex]]
 [[Category: Rattus norvegicus]]
-[[Category: Jardetzky, T.S.]]
+[[Category: Jardetzky, T S.]]
-[[Category: Thompson, T.B.]]
+[[Category: Thompson, T B.]]
-[[Category: Woodruff, T.K.]]
+[[Category: Woodruff, T K.]]
 [[Category: activin]]
 [[Category: actriib]]
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 [[Category: type ii]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 18:27:08 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:11:34 2008''