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<StructureSection load='1rew' size='340' side='right'caption='[[1rew]], [[Resolution|resolution]] 1.86&Aring;' scene=''>
<StructureSection load='1rew' size='340' side='right'caption='[[1rew]], [[Resolution|resolution]] 1.86&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1rew]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1REW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1REW FirstGlance]. <br>
<table><tr><td colspan='2'>[[1rew]] 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=1REW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1REW FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3bmp|3bmp]], [[1es7|1es7]], [[1reu|1reu]]</div></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]] 1.863&#8491;</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Transferase Transferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1, 2.7.11.8, 2.7.11.9, 2.7.11.10, 2.7.11.11, 2.7.11.12, 2.7.11.13, 2.7.11.21, 2.7.11.22, 2.7.11.24, 2.7.11.25, 2.7.11.30 and 2.7.12.1 2.7.11.1, 2.7.11.8, 2.7.11.9, 2.7.11.10, 2.7.11.11, 2.7.11.12, 2.7.11.13, 2.7.11.21, 2.7.11.22, 2.7.11.24, 2.7.11.25, 2.7.11.30 and 2.7.12.1] </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=1rew FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rew OCA], [https://pdbe.org/1rew PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rew RCSB], [https://www.ebi.ac.uk/pdbsum/1rew PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rew ProSAT]</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=1rew FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rew OCA], [https://pdbe.org/1rew PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rew RCSB], [https://www.ebi.ac.uk/pdbsum/1rew PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rew ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
[[https://www.uniprot.org/uniprot/BMR1A_HUMAN BMR1A_HUMAN]] Defects in BMPR1A are a cause of juvenile polyposis syndrome (JPS) [MIM:[https://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:[https://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:[https://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 ==
[[https://www.uniprot.org/uniprot/BMP2_HUMAN BMP2_HUMAN]] Induces cartilage and bone formation. [[https://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]]
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Transferase]]
[[Category: Keller S]]
[[Category: Keller, S]]
[[Category: Mueller TD]]
[[Category: Mueller, T D]]
[[Category: Nickel J]]
[[Category: Nickel, J]]
[[Category: Sebald W]]
[[Category: Sebald, W]]
[[Category: Zhang J-L]]
[[Category: Zhang, J L]]
[[Category: 3-finger toxin fold]]
[[Category: Bria-fold]]
[[Category: Hormone-growth factor-signaling protein complex]]
[[Category: Tgf-beta fold]]

Revision as of 09:03, 23 August 2023

Structural refinement of the complex of bone morphogenetic protein 2 and its type IA receptorStructural refinement of the complex of bone morphogenetic protein 2 and its type IA receptor

Structural highlights

1rew 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 1.863Å
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 protein-2 (BMP-2) and other members of the TGF-beta superfamily regulate the development, maintenance and regeneration of tissues and organs. Binding epitopes for these extracellular signaling proteins have been defined, but hot spots specifying binding affinity and specificity have so far not been identified. In this study, mutational and structural analyses show that epitopes of BMP-2 and the BRIA receptor form a new type of protein-protein interface. The main chain atoms of Leu 51 and Asp53 of BMP-2 represent a hot spot of binding to BRIA. The BMP-2 variant L51P was deficient in type I receptor binding only, whereas its overall structure and its binding to type II receptors and modulator proteins, such as noggin, were unchanged. Thus, the L51P substitution converts BMP-2 into a receptor-inactive inhibitor of noggin. These results are relevant for other proteins of the TGF-beta superfamily and provide useful clues for structure-based drug design.

Molecular recognition of BMP-2 and BMP receptor IA.,Keller S, Nickel J, Zhang JL, Sebald W, Mueller TD Nat Struct Mol Biol. 2004 May;11(5):481-8. Epub 2004 Apr 4. PMID:15064755[1]

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

See Also

References

  1. ↑ Keller S, Nickel J, Zhang JL, Sebald W, Mueller TD. Molecular recognition of BMP-2 and BMP receptor IA. Nat Struct Mol Biol. 2004 May;11(5):481-8. Epub 2004 Apr 4. PMID:15064755 doi:10.1038/nsmb756

1rew, resolution 1.86Å

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