1lx5
From Proteopedia
(New page: 200px<br /> <applet load="1lx5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lx5, resolution 3.30Å" /> '''Crystal Structure o...) |
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| - | [[Image:1lx5.gif|left|200px]]<br /> | + | [[Image:1lx5.gif|left|200px]]<br /><applet load="1lx5" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1lx5" size=" | + | |
caption="1lx5, resolution 3.30Å" /> | caption="1lx5, resolution 3.30Å" /> | ||
'''Crystal Structure of the BMP7/ActRII Extracellular Domain Complex'''<br /> | '''Crystal Structure of the BMP7/ActRII Extracellular Domain Complex'''<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== | ||
| - | 1LX5 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with NDG and NAG as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1LX5 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=NDG:'>NDG</scene> and <scene name='pdbligand=NAG:'>NAG</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LX5 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: ligand-receptor complex]] | [[Category: ligand-receptor complex]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:49:17 2008'' |
Revision as of 11:49, 21 February 2008
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Crystal Structure of the BMP7/ActRII Extracellular Domain Complex
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
1LX5 is a Protein complex structure of sequences from Homo sapiens and Mus musculus with and as ligands. 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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