1lxi
From Proteopedia
(New page: 200px<br /> <applet load="1lxi" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lxi, resolution 2.00Å" /> '''Refinement of BMP7 ...) |
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| - | [[Image:1lxi.gif|left|200px]]<br /> | + | [[Image:1lxi.gif|left|200px]]<br /><applet load="1lxi" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1lxi" size=" | + | |
caption="1lxi, resolution 2.00Å" /> | caption="1lxi, resolution 2.00Å" /> | ||
'''Refinement of BMP7 crystal structure'''<br /> | '''Refinement of BMP7 crystal structure'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Activins and bone morphogenetic proteins (BMPs) elicit diverse biological | + | Activins and bone morphogenetic proteins (BMPs) elicit diverse biological responses by signaling through two pairs of structurally related type I and type II receptors. Here we report the crystal structure of BMP7 in complex with the extracellular domain (ECD) of the activin type II receptor. Our structure produces a compelling four-receptor model, revealing that the types I and II receptor ECDs make no direct contacts. Nevertheless, we find that truncated receptors lacking their cytoplasmic domain retain the ability to cooperatively assemble in the cell membrane. Also, the affinity of BMP7 for its low-affinity type I receptor ECD increases 5-fold in the presence of its type II receptor ECD. Taken together, our results provide a view of the ligand-mediated cooperative assembly of BMP and activin receptors that does not rely on receptor-receptor contacts. |
==About this Structure== | ==About this Structure== | ||
| - | 1LXI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with NAG as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1LXI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] 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=1LXI OCA]. |
==Reference== | ==Reference== | ||
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[[Category: cystine-knot growth factor]] | [[Category: cystine-knot growth factor]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:49:23 2008'' |
Revision as of 11:49, 21 February 2008
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Refinement of BMP7 crystal structure
Overview
Activins and bone morphogenetic proteins (BMPs) elicit diverse biological responses by signaling through two pairs of structurally related type I and type II receptors. Here we report the crystal structure of BMP7 in complex with the extracellular domain (ECD) of the activin type II receptor. Our structure produces a compelling four-receptor model, revealing that the types I and II receptor ECDs make no direct contacts. Nevertheless, we find that truncated receptors lacking their cytoplasmic domain retain the ability to cooperatively assemble in the cell membrane. Also, the affinity of BMP7 for its low-affinity type I receptor ECD increases 5-fold in the presence of its type II receptor ECD. Taken together, our results provide a view of the ligand-mediated cooperative assembly of BMP and activin receptors that does not rely on receptor-receptor contacts.
About this Structure
1LXI is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.
Reference
The BMP7/ActRII extracellular domain complex provides new insights into the cooperative nature of receptor assembly., Greenwald J, Groppe J, Gray P, Wiater E, Kwiatkowski W, Vale W, Choe S, Mol Cell. 2003 Mar;11(3):605-17. PMID:12667445
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