2p6a
From Proteopedia
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| - | [[Image:2p6a.jpg|left|200px]] | + | [[Image:2p6a.jpg|left|200px]] |
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| - | '''The structure of the Activin:Follistatin 315 complex''' | + | {{Structure |
| + | |PDB= 2p6a |SIZE=350|CAPTION= <scene name='initialview01'>2p6a</scene>, resolution 3.400Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |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 Activin:Follistatin 315 complex''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2P6A is a [ | + | 2P6A 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=2P6A OCA]. |
==Reference== | ==Reference== | ||
| - | Structural and biophysical coupling of heparin and activin binding to follistatin isoform functions., Lerch TF, Shimasaki S, Woodruff TK, Jardetzky TS, J Biol Chem. 2007 May 25;282(21):15930-9. Epub 2007 Apr 3. PMID:[http:// | + | Structural and biophysical coupling of heparin and activin binding to follistatin isoform functions., Lerch TF, Shimasaki S, Woodruff TK, Jardetzky TS, J Biol Chem. 2007 May 25;282(21):15930-9. Epub 2007 Apr 3. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17409095 17409095] |
[[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 18:09:16 2008'' |
Revision as of 16:09, 20 March 2008
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| , resolution 3.400Å | |||||||
|---|---|---|---|---|---|---|---|
| Gene: | INHBA (Homo sapiens), FST (Homo sapiens) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
The structure of the Activin:Follistatin 315 complex
Contents |
Overview
Follistatin (FS) regulates transforming growth factor-beta superfamily ligands and is necessary for normal embryonic and ovarian follicle development. Follistatin is expressed as two splice variants (FS288 and FS315). Previous studies indicated differences in heparin binding between FS288 and FS315, potentially influencing the physiological functions and locations of these isoforms. We have determined the structure of the FS315-activin A complex and quantitatively compared heparin binding by the two isoforms. The FS315 complex structure shows that both isoforms inhibit activin similarly, but FS315 exhibits movements within follistatin domain 3 (FSD3) apparently linked to binding of the C-terminal extension. Surprisingly, the binding affinities of FS288 and FS315 for heparin are similar at lower ionic strengths with FS315 binding decreasing more sharply as a function of salt concentration. When bound to activin, FS315 binds heparin similarly to the FS288 isoform, consistent with the structure of the complex, in which the acidic residues of the C-terminal extension cannot interact with the heparin-binding site. Activin-induced binding of heparin is unique to the FS315 isoform and may stimulate clearance of FS315 complexes.
Disease
Known disease associated with this structure: Polycystic ovary syndrome OMIM:[136470]
About this Structure
2P6A is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structural and biophysical coupling of heparin and activin binding to follistatin isoform functions., Lerch TF, Shimasaki S, Woodruff TK, Jardetzky TS, J Biol Chem. 2007 May 25;282(21):15930-9. Epub 2007 Apr 3. PMID:17409095
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