1lx5

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[[Image:1lx5.gif|left|200px]]
 
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{{Structure
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==Crystal Structure of the BMP7/ActRII Extracellular Domain Complex==
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|PDB= 1lx5 |SIZE=350|CAPTION= <scene name='initialview01'>1lx5</scene>, resolution 3.30&Aring;
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<StructureSection load='1lx5' size='340' side='right'caption='[[1lx5]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</scene>
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<table><tr><td colspan='2'>[[1lx5]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LX5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LX5 FirstGlance]. <br>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.3&#8491;</td></tr>
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|GENE= BMP7 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]), ACVR2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
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|DOMAIN=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1lx5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lx5 OCA], [https://pdbe.org/1lx5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lx5 RCSB], [https://www.ebi.ac.uk/pdbsum/1lx5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lx5 ProSAT]</span></td></tr>
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|RELATEDENTRY=[[1lxi|1LXI]]
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1lx5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lx5 OCA], [http://www.ebi.ac.uk/pdbsum/1lx5 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1lx5 RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/BMP7_HUMAN BMP7_HUMAN] Induces cartilage and bone formation. May be the osteoinductive factor responsible for the phenomenon of epithelial osteogenesis. Plays a role in calcium regulation and bone homeostasis.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/lx/1lx5_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1lx5 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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'''Crystal Structure of the BMP7/ActRII Extracellular Domain Complex'''
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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<ref>PMID:12667445</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1lx5" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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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.
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*[[Bone morphogenetic protein 3D structures|Bone morphogenetic protein 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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1LX5 is a [[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]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LX5 OCA].
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__TOC__
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</StructureSection>
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==Reference==
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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:[http://www.ncbi.nlm.nih.gov/pubmed/12667445 12667445]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: Protein complex]]
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[[Category: Choe S]]
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[[Category: Choe, S.]]
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[[Category: Greenwald J]]
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[[Category: Greenwald, J.]]
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[[Category: Groppe J]]
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[[Category: Groppe, J.]]
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[[Category: Kwiatkowski W]]
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[[Category: Kwiatkowski, W.]]
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[[Category: ligand-receptor complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:08:31 2008''
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Current revision

Crystal Structure of the BMP7/ActRII Extracellular Domain Complex

PDB ID 1lx5

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