2b0u
From Proteopedia
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- | [[Image:2b0u.gif|left|200px]] | + | [[Image:2b0u.gif|left|200px]] |
- | + | ||
- | '''The Structure of the Follistatin:Activin Complex''' | + | {{Structure |
+ | |PDB= 2b0u |SIZE=350|CAPTION= <scene name='initialview01'>2b0u</scene>, resolution 2.800Å | ||
+ | |SITE= | ||
+ | |LIGAND= <scene name='pdbligand=IR3:IRIDIUM+(III)+ION'>IR3</scene>, <scene name='pdbligand=MLI:MALONATE+ION'>MLI</scene> and <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene> | ||
+ | |ACTIVITY= | ||
+ | |GENE= INHBA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]), FST ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
+ | }} | ||
+ | |||
+ | '''The Structure of the Follistatin:Activin Complex''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 2B0U is a [ | + | 2B0U is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B0U OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/16198295 16198295] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: tgf-beta]] | [[Category: tgf-beta]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:56:11 2008'' |
Revision as of 13:56, 20 March 2008
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, resolution 2.800Å | |||||||
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Ligands: | , and | ||||||
Gene: | INHBA (Homo sapiens), FST (Homo sapiens) | ||||||
Coordinates: | save as pdb, mmCIF, xml |
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. 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 Mar 20 15:56:11 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