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==COMPLEX BETWEEN BMP-2 AND TWO BMP RECEPTOR IA ECTODOMAINS==
==COMPLEX BETWEEN BMP-2 AND TWO BMP RECEPTOR IA ECTODOMAINS==
<StructureSection load='1es7' size='340' side='right' caption='[[1es7]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
<StructureSection load='1es7' size='340' side='right'caption='[[1es7]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1es7]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ES7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ES7 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1es7]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ES7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ES7 FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3bmp|3bmp]]</td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1es7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1es7 OCA], [http://pdbe.org/1es7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1es7 RCSB], [http://www.ebi.ac.uk/pdbsum/1es7 PDBsum]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1es7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1es7 OCA], [https://pdbe.org/1es7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1es7 RCSB], [https://www.ebi.ac.uk/pdbsum/1es7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1es7 ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
[[http://www.uniprot.org/uniprot/BMR1A_HUMAN BMR1A_HUMAN]] Defects in BMPR1A are a cause of juvenile polyposis syndrome (JPS) [MIM:[http://omim.org/entry/174900 174900]]; also known as juvenile intestinal polyposis (JIP). JPS is an autosomal dominant gastrointestinal hamartomatous polyposis syndrome in which patients are at risk for developing gastrointestinal cancers. The lesions are typified by a smooth histological appearance, predominant stroma, cystic spaces and lack of a smooth muscle core. Multiple juvenile polyps usually occur in a number of Mendelian disorders. Sometimes, these polyps occur without associated features as in JPS; here, polyps tend to occur in the large bowel and are associated with an increased risk of colon and other gastrointestinal cancers.<ref>PMID:11381269</ref> <ref>PMID:11536076</ref> <ref>PMID:12417513</ref> <ref>PMID:12136244</ref> <ref>PMID:12630959</ref>  Defects in BMPR1A are a cause of Cowden disease (CD) [MIM:[http://omim.org/entry/158350 158350]]. CD is an autosomal dominant cancer syndrome characterized by multiple hamartomas and by a high risk for breast, thyroid and endometrial cancers.<ref>PMID:11381269</ref> <ref>PMID:11536076</ref>  Defects in BMPR1A are the cause of hereditary mixed polyposis syndrome 2 (HMPS2) [MIM:[http://omim.org/entry/610069 610069]]. Hereditary mixed polyposis syndrome (HMPS) is characterized by atypical juvenile polyps, colonic adenomas, and colorectal carcinomas.<ref>PMID:11381269</ref>  Note=A microdeletion of chromosome 10q23 involving BMPR1A and PTEN is a cause of chromosome 10q23 deletion syndrome, which shows overlapping features of the following three disorders: Bannayan-Zonana syndrome, Cowden disease and juvenile polyposis syndrome.<ref>PMID:11381269</ref> 
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/BMP2_HUMAN BMP2_HUMAN]] Induces cartilage and bone formation. [[http://www.uniprot.org/uniprot/BMR1A_HUMAN BMR1A_HUMAN]] On ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators. Receptor for BMP-2 and BMP-4.  
[https://www.uniprot.org/uniprot/BMP2_HUMAN BMP2_HUMAN] Induces cartilage and bone formation.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/es/1es7_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/es/1es7_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </jmolCheckbox>
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</div>
</div>
<div class="pdbe-citations 1es7" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 1es7" style="background-color:#fffaf0;"></div>
==See Also==
*[[Bone morphogenetic protein 3D structures|Bone morphogenetic protein 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Dreyer, M K]]
[[Category: Large Structures]]
[[Category: Kirsch, T]]
[[Category: Dreyer MK]]
[[Category: Sebald, W]]
[[Category: Kirsch T]]
[[Category: Cytokine]]
[[Category: Sebald W]]
[[Category: Cytokine receptor]]
[[Category: Protein-protein complex]]
[[Category: Receptor-ligand complex]]
[[Category: Tgf beta superfamily]]
[[Category: Three finger toxin fold]]

Latest revision as of 09:35, 30 October 2024

COMPLEX BETWEEN BMP-2 AND TWO BMP RECEPTOR IA ECTODOMAINSCOMPLEX BETWEEN BMP-2 AND TWO BMP RECEPTOR IA ECTODOMAINS

Structural highlights

1es7 is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.9Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

BMP2_HUMAN Induces cartilage and bone formation.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Bone morphogenetic proteins (BMPs) belong to the large transforming growth factor-beta (TGF-beta) superfamily of multifunctional cytokines. BMP-2 can induce ectopic bone and cartilage formation in adult vertebrates and is involved in central steps in early embryonal development in animals. Signaling by these cytokines requires binding of two types of transmembrane serine/threonine receptor kinase chains classified as type I and type II. Here we report the crystal structure of human dimeric BMP-2 in complex with two high affinity BMP receptor IA extracellular domains (BRIAec). The receptor chains bind to the 'wrist' epitopes of the BMP-2 dimer and contact both BMP-2 monomers. No contacts exist between the receptor domains. The model reveals the structural basis for discrimination between type I and type II receptors and the variability of receptor-ligand interactions that is seen in BMP-TGF-beta systems.

Crystal structure of the BMP-2-BRIA ectodomain complex.,Kirsch T, Sebald W, Dreyer MK Nat Struct Biol. 2000 Jun;7(6):492-6. PMID:10881198[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ Kirsch T, Sebald W, Dreyer MK. Crystal structure of the BMP-2-BRIA ectodomain complex. Nat Struct Biol. 2000 Jun;7(6):492-6. PMID:10881198 doi:10.1038/75903

1es7, resolution 2.90Å

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