1bmp: Difference between revisions

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[[Image:1bmp.gif|left|200px]]
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{{STRUCTURE_1bmp|  PDB=1bmp  |  SCENE=  }}
'''BONE MORPHOGENETIC PROTEIN-7'''


==BONE MORPHOGENETIC PROTEIN-7==
<StructureSection load='1bmp' size='340' side='right'caption='[[1bmp]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1bmp]] is a 1 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=1BMP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BMP FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</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=1bmp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bmp OCA], [https://pdbe.org/1bmp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bmp RCSB], [https://www.ebi.ac.uk/pdbsum/1bmp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bmp ProSAT]</span></td></tr>
</table>
== Function ==
[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.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bm/1bmp_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1bmp ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
We report the three-dimensional structure of osteogenic protein 1 (OP-1, also known as bone morphogenetic protein 7) to 2.8-A resolution. OP-1 is a member of the transforming growth factor beta (TGF-beta) superfamily of proteins and is able to induce new bone formation in vivo. Members of this superfamily share sequence similarity in their C-terminal regions and are implicated in embryonic development and adult tissue repair. Our crystal structure makes possible the structural comparison between two members of the TGF-beta superfamily. We find that although there is limited sequence identity between OP-1 and TGF-beta 2, they share a common polypeptide fold. These results establish a basis for proposing the OP-1/TGF-beta 2 fold as the primary structural motif for the TGF-beta superfamily as a whole. Detailed comparison of the OP-1 and TGF-beta 2 structures has revealed striking differences that provide insights into how these growth factors interact with their receptors.


==Overview==
Three-dimensional structure of recombinant human osteogenic protein 1: structural paradigm for the transforming growth factor beta superfamily.,Griffith DL, Keck PC, Sampath TK, Rueger DC, Carlson WD Proc Natl Acad Sci U S A. 1996 Jan 23;93(2):878-83. PMID:8570652<ref>PMID:8570652</ref>
We report the three-dimensional structure of osteogenic protein 1 (OP-1, also known as bone morphogenetic protein 7) to 2.8-A resolution. OP-1 is a member of the transforming growth factor beta (TGF-beta) superfamily of proteins and is able to induce new bone formation in vivo. Members of this superfamily share sequence similarity in their C-terminal regions and are implicated in embryonic development and adult tissue repair. Our crystal structure makes possible the structural comparison between two members of the TGF-beta superfamily. We find that although there is limited sequence identity between OP-1 and TGF-beta 2, they share a common polypeptide fold. These results establish a basis for proposing the OP-1/TGF-beta 2 fold as the primary structural motif for the TGF-beta superfamily as a whole. Detailed comparison of the OP-1 and TGF-beta 2 structures has revealed striking differences that provide insights into how these growth factors interact with their receptors.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1BMP is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BMP OCA].
</div>
<div class="pdbe-citations 1bmp" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Three-dimensional structure of recombinant human osteogenic protein 1: structural paradigm for the transforming growth factor beta superfamily., Griffith DL, Keck PC, Sampath TK, Rueger DC, Carlson WD, Proc Natl Acad Sci U S A. 1996 Jan 23;93(2):878-83. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8570652 8570652]
*[[Bone morphogenetic protein 3D structures|Bone morphogenetic protein 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Griffith, D L.]]
[[Category: Griffith DL]]
[[Category: Scott, D L.]]
[[Category: Scott DL]]
[[Category: Bone]]
[[Category: Cartilage]]
[[Category: Cytokine]]
[[Category: Glycoprotein]]
[[Category: Morphogen]]
[[Category: Transforming growth factor]]
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