2b0u: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[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== | ||
| Line 10: | Line 19: | ||
==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]] | ||
| Line 30: | Line 39: | ||
[[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
| |||||||||||||
| 2b0u, resolution 2.800Å | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Ligands: | IR3, MLI and MPD | ||||||||||||
| Gene: | INHBA (Homo sapiens), FST (Homo sapiens) | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
The Structure of the Follistatin:Activin Complex
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
