1bte
From Proteopedia
(New page: 200px<br /><applet load="1bte" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bte, resolution 1.5Å" /> '''CRYSTAL STRUCTURE OF ...) |
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| - | [[Image:1bte.gif|left|200px]]<br /><applet load="1bte" size=" | + | [[Image:1bte.gif|left|200px]]<br /><applet load="1bte" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1bte, resolution 1.5Å" /> | caption="1bte, resolution 1.5Å" /> | ||
'''CRYSTAL STRUCTURE OF THE EXTRACELLULAR DOMAIN OF THE TYPE II ACTIVIN RECEPTOR'''<br /> | '''CRYSTAL STRUCTURE OF THE EXTRACELLULAR DOMAIN OF THE TYPE II ACTIVIN RECEPTOR'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The transforming growth factor beta (TGFbeta) superfamily of cytokines | + | The transforming growth factor beta (TGFbeta) superfamily of cytokines elicit diverse biological responses by interacting with two distinct, but structurally related transmembrane receptor serine kinases (type I and type II). The binding of these dimeric ligands to the type II receptor is the first event in transmembrane signaling for this family. Here we report the 1.5 A resolution crystal structure of the extracellular ligand-binding domain of the type II activin receptor (ActRII-ECD), which reveals a fold similar to that of a class of toxins known as three-finger toxins. This fold is primarily dictated by disulfide bonds formed by eight conserved cysteines, with a characteristic spacing, and thus is likely to be shared by most of the type I and II receptors for the TGFbeta family. Sequence comparison with an evolutionarily distant activin binding-protein identifies several conserved residues, including two hydrophobic clusters that may form binding surfaces for activin and the type I receptor. |
==About this Structure== | ==About this Structure== | ||
| - | 1BTE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with NAG as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1BTE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=NAG:'>NAG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BTE OCA]. |
==Reference== | ==Reference== | ||
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[[Category: three-finger toxin]] | [[Category: three-finger toxin]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:58:53 2008'' |
Revision as of 09:58, 21 February 2008
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CRYSTAL STRUCTURE OF THE EXTRACELLULAR DOMAIN OF THE TYPE II ACTIVIN RECEPTOR
Overview
The transforming growth factor beta (TGFbeta) superfamily of cytokines elicit diverse biological responses by interacting with two distinct, but structurally related transmembrane receptor serine kinases (type I and type II). The binding of these dimeric ligands to the type II receptor is the first event in transmembrane signaling for this family. Here we report the 1.5 A resolution crystal structure of the extracellular ligand-binding domain of the type II activin receptor (ActRII-ECD), which reveals a fold similar to that of a class of toxins known as three-finger toxins. This fold is primarily dictated by disulfide bonds formed by eight conserved cysteines, with a characteristic spacing, and thus is likely to be shared by most of the type I and II receptors for the TGFbeta family. Sequence comparison with an evolutionarily distant activin binding-protein identifies several conserved residues, including two hydrophobic clusters that may form binding surfaces for activin and the type I receptor.
About this Structure
1BTE is a Single protein structure of sequence from Mus musculus with as ligand. Full crystallographic information is available from OCA.
Reference
Three-finger toxin fold for the extracellular ligand-binding domain of the type II activin receptor serine kinase., Greenwald J, Fischer WH, Vale WW, Choe S, Nat Struct Biol. 1999 Jan;6(1):18-22. PMID:9886286
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