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2b0u
From Proteopedia
(New page: 200px<br /> <applet load="2b0u" size="450" color="white" frame="true" align="right" spinBox="true" caption="2b0u, resolution 2.800Å" /> '''The Structure of t...) |
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| - | [[Image:2b0u.gif|left|200px]]<br /> | + | [[Image:2b0u.gif|left|200px]]<br /><applet load="2b0u" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="2b0u" size=" | + | |
caption="2b0u, resolution 2.800Å" /> | caption="2b0u, resolution 2.800Å" /> | ||
'''The Structure of the Follistatin:Activin Complex'''<br /> | '''The Structure of the Follistatin:Activin Complex'''<br /> | ||
==Overview== | ==Overview== | ||
| - | TGF-beta ligands stimulate diverse cellular differentiation and growth | + | TGF-beta ligands stimulate diverse cellular differentiation and growth responses by signaling through type I and II receptors. Ligand antagonists, such as follistatin, block signaling and are essential regulators of physiological responses. Here we report the structure of activin A, a TGF-beta ligand, bound to the high-affinity antagonist follistatin. Two follistatin molecules encircle activin, neutralizing the ligand by burying one-third of its residues and its receptor binding sites. Previous studies have suggested that type I receptor binding would not be blocked by follistatin, but the crystal structure reveals that the follistatin N-terminal domain has an unexpected fold that mimics a universal type I receptor motif and occupies this receptor binding site. The formation of follistatin:BMP:type I receptor complexes can be explained by the stoichiometric and geometric arrangement of the activin:follistatin complex. The mode of ligand binding by follistatin has important implications for its ability to neutralize homo- and heterodimeric ligands of this growth factor family. |
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2B0U is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with IR3, MLI and MPD as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 2B0U is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=IR3:'>IR3</scene>, <scene name='pdbligand=MLI:'>MLI</scene> and <scene name='pdbligand=MPD:'>MPD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B0U OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Cook, R | + | [[Category: Cook, R W.]] |
| - | [[Category: Jardetzky, T | + | [[Category: Jardetzky, T S.]] |
| - | [[Category: Lerch, T | + | [[Category: Lerch, T F.]] |
| - | [[Category: Thompson, T | + | [[Category: Thompson, T B.]] |
| - | [[Category: Woodruff, T | + | [[Category: Woodruff, T K.]] |
[[Category: IR3]] | [[Category: IR3]] | ||
[[Category: MLI]] | [[Category: MLI]] | ||
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[[Category: tgf-beta]] | [[Category: tgf-beta]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:33:02 2008'' |
Revision as of 14:33, 21 February 2008
|
The Structure of the Follistatin:Activin Complex
Contents |
Overview
TGF-beta ligands stimulate diverse cellular differentiation and growth responses by signaling through type I and II receptors. Ligand antagonists, such as follistatin, block signaling and are essential regulators of physiological responses. Here we report the structure of activin A, a TGF-beta ligand, bound to the high-affinity antagonist follistatin. Two follistatin molecules encircle activin, neutralizing the ligand by burying one-third of its residues and its receptor binding sites. Previous studies have suggested that type I receptor binding would not be blocked by follistatin, but the crystal structure reveals that the follistatin N-terminal domain has an unexpected fold that mimics a universal type I receptor motif and occupies this receptor binding site. The formation of follistatin:BMP:type I receptor complexes can be explained by the stoichiometric and geometric arrangement of the activin:follistatin complex. The mode of ligand binding by follistatin has important implications for its ability to neutralize homo- and heterodimeric ligands of this growth factor family.
Disease
Known disease associated with this structure: Polycystic ovary syndrome OMIM:[136470]
About this Structure
2B0U is a Protein complex structure of sequences from Homo sapiens with , and as ligands. Full crystallographic information is available from OCA.
Reference
The structure of the follistatin:activin complex reveals antagonism of both type I and type II receptor binding., Thompson TB, Lerch TF, Cook RW, Woodruff TK, Jardetzky TS, Dev Cell. 2005 Oct;9(4):535-43. PMID:16198295
Page seeded by OCA on Thu Feb 21 16:33:02 2008
Categories: Homo sapiens | Protein complex | Cook, R W. | Jardetzky, T S. | Lerch, T F. | Thompson, T B. | Woodruff, T K. | IR3 | MLI | MPD | Activin | Follistatin | Inhibin | Morphogen | Tgf-beta
